ID   VPS39_HUMAN             Reviewed;         886 AA.
AC   Q96JC1; O94869; Q71SQ6; Q7Z3V3; Q96B93; Q96RM0;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   28-JUN-2023, entry version 173.
DE   RecName: Full=Vam6/Vps39-like protein {ECO:0000305};
DE   AltName: Full=TRAP1-like protein;
DE            Short=hVam6p;
GN   Name=VPS39 {ECO:0000312|HGNC:HGNC:20593}; Synonyms=KIAA0770, TLP, VAM6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
RP   HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11448994; DOI=10.1083/jcb.200102142;
RA   Caplan S., Hartnell L.M., Aguilar R.C., Naslavsky N., Bonifacino J.S.;
RT   "Human Vam6p promotes lysosome clustering and fusion in vivo.";
RL   J. Cell Biol. 154:109-122(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Dell'Angelica E.C.;
RT   "A human homolog of yeast Vps39.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Endometrial tumor;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 101-886 (ISOFORMS 1/2).
RC   TISSUE=Lung, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, INTERACTION WITH ACVR2B; SMAD4; TGFBR1 AND TGFBR2, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12941698; DOI=10.1093/emboj/cdg428;
RA   Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
RA   McNally J.G., Roberts A.B.;
RT   "TLP, a novel modulator of TGF-beta signaling, has opposite effects on
RT   Smad2- and Smad3-dependent signaling.";
RL   EMBO J. 22:4465-4477(2003).
RN   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
RN   [11]
RP   REVIEW ON THE HOPS AND CORVET COMPLEXES.
RX   PubMed=23351085; DOI=10.1111/febs.12151;
RA   Solinger J.A., Spang A.;
RT   "Tethering complexes in the endocytic pathway: CORVET and HOPS.";
RL   FEBS J. 280:2743-2757(2013).
RN   [12]
RP   INTERACTION WITH VPS11.
RX   PubMed=23901104; DOI=10.1073/pnas.1307074110;
RA   Graham S.C., Wartosch L., Gray S.R., Scourfield E.J., Deane J.E.,
RA   Luzio J.P., Owen D.J.;
RT   "Structural basis of Vps33A recruitment to the human HOPS complex by
RT   Vps16.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:13345-13350(2013).
RN   [13]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23167963; DOI=10.1111/tra.12027;
RA   Pols M.S., ten Brink C., Gosavi P., Oorschot V., Klumperman J.;
RT   "The HOPS proteins hVps41 and hVps39 are required for homotypic and
RT   heterotypic late endosome fusion.";
RL   Traffic 14:219-232(2013).
RN   [14]
RP   SUBUNIT, AND INTERACTION WITH PLEKHM2.
RX   PubMed=25908847; DOI=10.1242/jcs.162651;
RA   Khatter D., Raina V.B., Dwivedi D., Sindhwani A., Bahl S., Sharma M.;
RT   "The small GTPase Arl8b regulates assembly of the mammalian HOPS complex on
RT   lysosomes.";
RL   J. Cell Sci. 128:1746-1761(2015).
RN   [15]
RP   FUNCTION, AND FUNCTION OF THE HOPS COMPLEX.
RX   PubMed=25783203; DOI=10.1111/tra.12283;
RA   Wartosch L., Guenesdogan U., Graham S.C., Luzio J.P.;
RT   "Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion
RT   with Endosomes and Autophagosomes.";
RL   Traffic 16:727-742(2015).
RN   [16]
RP   INTERACTION WITH STX17.
RX   PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA   Miao G., Zhang Y., Chen D., Zhang H.;
RT   "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT   by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL   Mol. Cell 0:0-0(2019).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH SARS-COV-2 ORF3A PROTEIN (MICROBIAL
RP   INFECTION).
RX   PubMed=33422265; DOI=10.1016/j.devcel.2020.12.010;
RA   Miao G., Zhao H., Li Y., Ji M., Chen Y., Shi Y., Bi Y., Wang P., Zhang H.;
RT   "ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
RT   assembly of the SNARE complex required for autolysosome formation.";
RL   Dev. Cell 56:427-442(2020).
CC   -!- FUNCTION: Regulator of TGF-beta/activin signaling, inhibiting
CC       SMAD3- and activating SMAD2-dependent transcription. Acts by
CC       interfering with SMAD3/SMAD4 complex formation, this would lead to
CC       inhibition of SMAD3-dependent transcription and relieve SMAD3
CC       inhibition of SMAD2-dependent promoters, thus increasing SMAD2-
CC       dependent transcription. Does not affect TGF-beta-induced SMAD2 or
CC       SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation.
CC       {ECO:0000269|PubMed:12941698}.
CC   -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC       lysosomal compartments including the endocytic membrane transport and
CC       autophagic pathways. Acts as a component of the putative HOPS endosomal
CC       tethering complex which is proposed to be involved in the Rab5-to-Rab7
CC       endosome conversion probably implicating MON1A/B, and via binding
CC       SNAREs and SNARE complexes to mediate tethering and docking events
CC       during SNARE-mediated membrane fusion. The HOPS complex is proposed to
CC       be recruited to Rab7 on the late endosomal membrane and to regulate
CC       late endocytic, phagocytic and autophagic traffic towards lysosomes
CC       (PubMed:23351085). Involved in homotypic vesicle fusions between late
CC       endosomes and in heterotypic fusions between late endosomes and
CC       lysosomes (PubMed:11448994, PubMed:23351085, PubMed:23167963). Required
CC       for fusion of endosomes and autophagosomes with lysosomes
CC       (PubMed:25783203). {ECO:0000269|PubMed:11448994,
CC       ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:25783203,
CC       ECO:0000269|PubMed:33422265, ECO:0000305|PubMed:23351085}.
CC   -!- SUBUNIT: Homooligomer (PubMed:11448994). Interacts with TGFBR2 and,
CC       less efficiently, with TGFBR1; interaction with TGFBR2 is independent
CC       of the receptor kinase activity and of the presence of TGF-beta. Also
CC       interacts with ACVR2B, but not with BMPR2. Interacts with SMAD4,
CC       preferentially following TGF-beta treatment. Does not interact with
CC       SAMD2 or SMAD3 (PubMed:12941698). Component of the putative homotypic
CC       fusion and vacuole protein sorting (HOPS) complex; the core of which
CC       composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, is
CC       associated with VPS39 and VPS41 (PubMed:23351085, PubMed:23901104,
CC       PubMed:25908847, PubMed:33422265). Interacts with PLEKHM2; involved in
CC       VPS39 recruitment to ARL8B-containing lysosomes (PubMed:25908847).
CC       Associates with adaptor protein complex 3 (AP-3) and clathrin:AP-3
CC       complexes (By similarity). Interacts with STX17; this interaction is
CC       increased in the absence of TMEM39A (PubMed:31806350).
CC       {ECO:0000250|UniProtKB:Q8R5L3, ECO:0000269|PubMed:11448994,
CC       ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:23901104,
CC       ECO:0000269|PubMed:25908847, ECO:0000269|PubMed:31806350,
CC       ECO:0000269|PubMed:33422265, ECO:0000305|PubMed:23351085,
CC       ECO:0000305|PubMed:25908847}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC       CoV-2 ORF3A protein; the interaction is direct and sequestrates VPS39,
CC       thereby preventing HOPS complex from interacting with the
CC       autophagosomal SNARE protein STX17 (PubMed:33422265). ORF3A enhances
CC       the interaction of VPS39 with VPS11 and VPS18, while its interaction
CC       with the VPS16:VPS33A module is attenuated (PubMed:23167963).
CC       {ECO:0000269|PubMed:23167963, ECO:0000269|PubMed:33422265}.
CC   -!- INTERACTION:
CC       Q96JC1; Q9Y4G2: PLEKHM1; NbExp=5; IntAct=EBI-1050197, EBI-473814;
CC       Q96JC1; P51149: RAB7A; NbExp=2; IntAct=EBI-1050197, EBI-1056089;
CC       Q96JC1; P56962: STX17; NbExp=2; IntAct=EBI-1050197, EBI-2797775;
CC       Q96JC1; Q9P253: VPS18; NbExp=2; IntAct=EBI-1050197, EBI-1053363;
CC       Q96JC1; P0DTC3: 3a; Xeno; NbExp=18; IntAct=EBI-1050197, EBI-25475894;
CC       Q96JC1-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11962886, EBI-1105213;
CC       Q96JC1-2; Q9H270: VPS11; NbExp=4; IntAct=EBI-11962886, EBI-373380;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome membrane
CC       {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:17897319,
CC       ECO:0000269|PubMed:23167963}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:11448994}. Late endosome membrane
CC       {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:23167963}; Peripheral
CC       membrane protein {ECO:0000305|PubMed:11448994}. Note=Colocalizes with
CC       TGFBR1 and TGFBR2 in cytoplasmic vesicular structures and most
CC       prominently in cortical vesicles. {ECO:0000269|PubMed:12941698}.
CC   -!- SUBCELLULAR LOCATION: Note=(Microbial infection) Sequestrated at the
CC       late endosome by SARS coronavirus-2/SARS-CoV-2 ORF3A protein.
CC       {ECO:0000269|PubMed:33422265}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96JC1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96JC1-2; Sequence=VSP_004075;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in heart,
CC       skeletal muscle, kidney, pancreas, brain, placenta and spleen.
CC       {ECO:0000269|PubMed:11448994, ECO:0000269|PubMed:12941698}.
CC   -!- SIMILARITY: Belongs to the VAM6/VPS39 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34490.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF280814; AAK72222.1; -; mRNA.
DR   EMBL; AF334400; AAK58862.1; -; Genomic_DNA.
DR   EMBL; AF281052; AAQ05978.1; -; mRNA.
DR   EMBL; AB018313; BAA34490.2; ALT_INIT; mRNA.
DR   EMBL; BX537404; CAD97646.1; -; mRNA.
DR   EMBL; AC036103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471125; EAW92536.1; -; Genomic_DNA.
DR   EMBL; BC015817; AAH15817.2; -; mRNA.
DR   EMBL; BC068559; AAH68559.1; -; mRNA.
DR   CCDS; CCDS10083.1; -. [Q96JC1-2]
DR   CCDS; CCDS73710.1; -. [Q96JC1-1]
DR   RefSeq; NP_001288067.1; NM_001301138.1. [Q96JC1-1]
DR   RefSeq; NP_056104.2; NM_015289.3. [Q96JC1-2]
DR   PDB; 6ZE9; X-ray; 2.90 A; A/B/C=851-886.
DR   PDBsum; 6ZE9; -.
DR   AlphaFoldDB; Q96JC1; -.
DR   SMR; Q96JC1; -.
DR   BioGRID; 116925; 50.
DR   ComplexPortal; CPX-6212; HOPS tethering complex.
DR   CORUM; Q96JC1; -.
DR   IntAct; Q96JC1; 37.
DR   MINT; Q96JC1; -.
DR   STRING; 9606.ENSP00000335193; -.
DR   iPTMnet; Q96JC1; -.
DR   PhosphoSitePlus; Q96JC1; -.
DR   BioMuta; VPS39; -.
DR   DMDM; 66774218; -.
DR   EPD; Q96JC1; -.
DR   jPOST; Q96JC1; -.
DR   MassIVE; Q96JC1; -.
DR   MaxQB; Q96JC1; -.
DR   PaxDb; Q96JC1; -.
DR   PeptideAtlas; Q96JC1; -.
DR   ProteomicsDB; 76939; -. [Q96JC1-1]
DR   ProteomicsDB; 76940; -. [Q96JC1-2]
DR   Antibodypedia; 23540; 124 antibodies from 25 providers.
DR   DNASU; 23339; -.
DR   Ensembl; ENST00000318006.10; ENSP00000326534.5; ENSG00000166887.16. [Q96JC1-2]
DR   Ensembl; ENST00000348544.4; ENSP00000335193.5; ENSG00000166887.16. [Q96JC1-1]
DR   GeneID; 23339; -.
DR   KEGG; hsa:23339; -.
DR   MANE-Select; ENST00000318006.10; ENSP00000326534.5; NM_015289.5; NP_056104.2. [Q96JC1-2]
DR   UCSC; uc001zpc.4; human. [Q96JC1-1]
DR   AGR; HGNC:20593; -.
DR   CTD; 23339; -.
DR   DisGeNET; 23339; -.
DR   GeneCards; VPS39; -.
DR   HGNC; HGNC:20593; VPS39.
DR   HPA; ENSG00000166887; Low tissue specificity.
DR   MIM; 612188; gene.
DR   neXtProt; NX_Q96JC1; -.
DR   OpenTargets; ENSG00000166887; -.
DR   PharmGKB; PA134945163; -.
DR   VEuPathDB; HostDB:ENSG00000166887; -.
DR   eggNOG; KOG2063; Eukaryota.
DR   GeneTree; ENSGT00530000063596; -.
DR   HOGENOM; CLU_004190_1_1_1; -.
DR   InParanoid; Q96JC1; -.
DR   OMA; LFRLPNF; -.
DR   OrthoDB; 38195at2759; -.
DR   PhylomeDB; Q96JC1; -.
DR   TreeFam; TF105803; -.
DR   PathwayCommons; Q96JC1; -.
DR   Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR   SignaLink; Q96JC1; -.
DR   SIGNOR; Q96JC1; -.
DR   BioGRID-ORCS; 23339; 123 hits in 1185 CRISPR screens.
DR   ChiTaRS; VPS39; human.
DR   GeneWiki; VPS39; -.
DR   GenomeRNAi; 23339; -.
DR   Pharos; Q96JC1; Tbio.
DR   PRO; PR:Q96JC1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q96JC1; protein.
DR   Bgee; ENSG00000166887; Expressed in right uterine tube and 199 other tissues.
DR   ExpressionAtlas; Q96JC1; baseline and differential.
DR   Genevisible; Q96JC1; HS.
DR   GO; GO:0030123; C:AP-3 adaptor complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:1902501; C:lysosomal HOPS complex; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; IDA:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:1902774; P:late endosome to lysosome transport; IDA:UniProtKB.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; NAS:ComplexPortal.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR   InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR   InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR   PANTHER; PTHR12894; CNH DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR12894:SF27; VAM6/VPS39-LIKE PROTEIN; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF10366; Vps39_1; 1.
DR   Pfam; PF10367; Vps39_2; 1.
DR   SMART; SM00036; CNH; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50219; CNH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autophagy; Cytoplasm; Endosome;
KW   Host-virus interaction; Lysosome; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..886
FT                   /note="Vam6/Vps39-like protein"
FT                   /id="PRO_0000065901"
FT   DOMAIN          15..294
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REPEAT          573..750
FT                   /note="CHCR"
FT   VAR_SEQ         47..58
FT                   /note="VPADVASPESGS -> G (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:9872452,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_004075"
FT   CONFLICT        135
FT                   /note="R -> Q (in Ref. 1; AAK72222)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="D -> G (in Ref. 5; CAD97646)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        846
FT                   /note="I -> T (in Ref. 5; CAD97646)"
FT                   /evidence="ECO:0000305"
FT   STRAND          851..858
FT                   /evidence="ECO:0007829|PDB:6ZE9"
FT   STRAND          865..867
FT                   /evidence="ECO:0007829|PDB:6ZE9"
FT   STRAND          871..877
FT                   /evidence="ECO:0007829|PDB:6ZE9"
FT   HELIX           883..885
FT                   /evidence="ECO:0007829|PDB:6ZE9"
SQ   SEQUENCE   886 AA;  101809 MW;  E5A40A3C787EB112 CRC64;
     MHDAFEPVPI LEKLPLQIDC LAAWEEWLLV GTKQGHLLLY RIRKDVVPAD VASPESGSCN
     RFEVTLEKSN KNFSKKIQQI HVVSQFKILV SLLENNIYVH DLLTFQQITT VSKAKGASLF
     TCDLQHTETG EEVLRMCVAV KKKLQLYFWK DREFHELQGD FSVPDVPKSM AWCENSICVG
     FKRDYYLIRV DGKGSIKELF PTGKQLEPLV APLADGKVAV GQDDLTVVLN EEGICTQKCA
     LNWTDIPVAM EHQPPYIIAV LPRYVEIRTF EPRLLVQSIE LQRPRFITSG GSNIIYVASN
     HFVWRLIPVP MATQIQQLLQ DKQFELALQL AEMKDDSDSE KQQQIHHIKN LYAFNLFCQK
     RFDESMQVFA KLGTDPTHVM GLYPDLLPTD YRKQLQYPNP LPVLSGAELE KAHLALIDYL
     TQKRSQLVKK LNDSDHQSST SPLMEGTPTI KSKKKLLQII DTTLLKCYLH TNVALVAPLL
     RLENNHCHIE ESEHVLKKAH KYSELIILYE KKGLHEKALQ VLVDQSKKAN SPLKGHERTV
     QYLQHLGTEN LHLIFSYSVW VLRDFPEDGL KIFTEDLPEV ESLPRDRVLG FLIENFKGLA
     IPYLEHIIHV WEETGSRFHN CLIQLYCEKV QGLMKEYLLS FPAGKTPVPA GEEEGELGEY
     RQKLLMFLEI SSYYDPGRLI CDFPFDGLLE ERALLLGRMG KHEQALFIYV HILKDTRMAE
     EYCHKHYDRN KDGNKDVYLS LLRMYLSPPS IHCLGPIKLE LLEPKANLQA ALQVLELHHS
     KLDTTKALNL LPANTQINDI RIFLEKVLEE NAQKKRFNQV LKNLLHAEFL RVQEERILHQ
     QVKCIITEEK VCMVCKKKIG NSAFARYPNG VVVHYFCSKE VNPADT
//