ID   SNP29_HUMAN             Reviewed;         258 AA.
AC   O95721;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   28-JUN-2023, entry version 200.
DE   RecName: Full=Synaptosomal-associated protein 29 {ECO:0000312|HGNC:HGNC:11133};
DE            Short=SNAP-29 {ECO:0000312|HGNC:HGNC:11133};
DE   AltName: Full=Soluble 29 kDa NSF attachment protein {ECO:0000312|HGNC:HGNC:11133};
DE   AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN   Name=SNAP29 {ECO:0000312|HGNC:HGNC:11133};
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
RA   Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA   Scheller R.H.;
RT   "Three novel proteins of the syntaxin/SNAP-25 family.";
RL   J. Biol. Chem. 273:34171-34179(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schardt A., Kraemer E.-M., Werner H., Nave K.-A.;
RT   "Genomic organization of the human SNAP29 gene.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [6]
RP   INVOLVEMENT IN CEDNIK.
RX   PubMed=15968592; DOI=10.1086/432556;
RA   Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D.,
RA   Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H., O'brien T.J.,
RA   Bercovich D., Shalev S., Geiger D., Bergman R., Horowitz M., Mandel H.;
RT   "A mutation in SNAP29, coding for a SNARE protein involved in intracellular
RT   trafficking, causes a novel neurocutaneous syndrome characterized by
RT   cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar
RT   keratoderma.";
RL   Am. J. Hum. Genet. 77:242-251(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   FUNCTION IN AUTOPHAGY, AND INTERACTION WITH VAMP8 AND STX17.
RX   PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA   Itakura E., Kishi-Itakura C., Mizushima N.;
RT   "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes
RT   for fusion with endosomes/lysosomes.";
RL   Cell 151:1256-1269(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-114; THR-130;
RP   THR-137; SER-163; SER-182; SER-185; SER-204 AND SER-210, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25686250; DOI=10.1038/ncb3109;
RA   Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA   Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA   Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RT   "Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary
RT   vesicle formation.";
RL   Nat. Cell Biol. 17:228-240(2015).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
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   [14]
RP   INTERACTION WITH HANTAAN HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX   PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA   Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA   Zhang F.;
RT   "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT   Autophagy Flux to Restrain Host Innate Immune Responses.";
RL   Cell Rep. 27:2075-2091.e5(2019).
RN   [15]
RP   INTERACTION WITH EIPR1.
RX   PubMed=27440922; DOI=10.1091/mbc.e16-04-0209;
RA   Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
RT   "TSSC1 is novel component of the endosomal retrieval machinery.";
RL   Mol. Biol. Cell 27:2867-2878(2016).
RN   [16]
RP   INTERACTION WITH STX17 (MICROBIAL 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).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 39-116 AND 194-258 IN COMPLEX WITH
RP   STX17 AND VAMP8, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=25686604; DOI=10.1038/nature14147;
RA   Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M.,
RA   Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.;
RT   "ATG14 promotes membrane tethering and fusion of autophagosomes to
RT   endolysosomes.";
RL   Nature 520:563-566(2015).
CC   -!- FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment
CC       protein receptors, are essential proteins for fusion of cellular
CC       membranes. SNAREs localized on opposing membranes assemble to form a
CC       trans-SNARE complex, an extended, parallel four alpha-helical bundle
CC       that drives membrane fusion. SNAP29 is a SNARE involved in autophagy
CC       through the direct control of autophagosome membrane fusion with the
CC       lysososome membrane. Also plays a role in ciliogenesis by regulating
CC       membrane fusions. {ECO:0000269|PubMed:23217709,
CC       ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}.
CC   -!- SUBUNIT: Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17,
CC       involved in fusion of autophagosome with lysosome (PubMed:23217709,
CC       PubMed:25686604). Interacts with multiple syntaxins including STX6 (By
CC       similarity). Interacts with EIPR1 (PubMed:27440922). Interacts with
CC       STX17; this interaction is increased in the absence of TMEM39A
CC       (PubMed:31806350, PubMed:33422265). {ECO:0000250|UniProtKB:Q9Z2P6,
CC       ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604,
CC       ECO:0000269|PubMed:27440922, ECO:0000269|PubMed:31806350,
CC       ECO:0000269|PubMed:33422265}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC       nucleoprotein; this interaction prevents the breakdown of the viral
CC       glycoprotein N by virus-triggered autophagy.
CC       {ECO:0000269|PubMed:31091447}.
CC   -!- SUBUNIT: (Microbial infection) The interaction with STX17 is decreased
CC       in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A protein.
CC       {ECO:0000269|PubMed:33422265}.
CC   -!- INTERACTION:
CC       O95721; P54253: ATXN1; NbExp=3; IntAct=EBI-490676, EBI-930964;
CC       O95721; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-490676, EBI-3866319;
CC       O95721; Q9H4M9: EHD1; NbExp=3; IntAct=EBI-490676, EBI-490691;
CC       O95721; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-490676, EBI-10175124;
CC       O95721; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-490676, EBI-2870039;
CC       O95721; P42858: HTT; NbExp=3; IntAct=EBI-490676, EBI-466029;
CC       O95721; Q9H115: NAPB; NbExp=8; IntAct=EBI-490676, EBI-3921185;
CC       O95721; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-490676, EBI-741158;
CC       O95721; O15294: OGT; NbExp=2; IntAct=EBI-490676, EBI-539828;
CC       O95721; Q86Y82: STX12; NbExp=5; IntAct=EBI-490676, EBI-2691717;
CC       O95721; O14662-5: STX16; NbExp=3; IntAct=EBI-490676, EBI-9089968;
CC       O95721; P56962: STX17; NbExp=10; IntAct=EBI-490676, EBI-2797775;
CC       O95721; P61266: STX1B; NbExp=3; IntAct=EBI-490676, EBI-9071709;
CC       O95721; P32856-2: STX2; NbExp=3; IntAct=EBI-490676, EBI-11956649;
CC       O95721; Q13277: STX3; NbExp=3; IntAct=EBI-490676, EBI-1394295;
CC       O95721; O43752: STX6; NbExp=3; IntAct=EBI-490676, EBI-2695795;
CC       O95721; Q13114: TRAF3; NbExp=4; IntAct=EBI-490676, EBI-357631;
CC       O95721; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-490676, EBI-12003468;
CC       O95721; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-490676, EBI-18122152;
CC       O95721; P23763: VAMP1; NbExp=3; IntAct=EBI-490676, EBI-10201335;
CC       O95721; P63027: VAMP2; NbExp=3; IntAct=EBI-490676, EBI-520113;
CC       O95721; Q15836: VAMP3; NbExp=3; IntAct=EBI-490676, EBI-722343;
CC       O95721; O75379-2: VAMP4; NbExp=3; IntAct=EBI-490676, EBI-10187996;
CC       O95721; O95183: VAMP5; NbExp=9; IntAct=EBI-490676, EBI-10191195;
CC       O95721; Q9BV40: VAMP8; NbExp=6; IntAct=EBI-490676, EBI-727028;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23217709}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane
CC       protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000269|PubMed:25686604}; Peripheral membrane protein
CC       {ECO:0000305}. Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:25686250}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via
CC       interaction with syntaxins, but a significant portion is cytoplasmic.
CC       Localizes to the ciliary pocket from where the cilium protrudes.
CC       {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250}.
CC   -!- TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung,
CC       placenta, skeletal muscle, spleen and pancreas.
CC       {ECO:0000269|PubMed:9852078}.
CC   -!- DISEASE: Cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar
CC       keratoderma syndrome (CEDNIK) [MIM:609528]: A neurocutaneous syndrome
CC       characterized by cerebral dysgenesis, neuropathy, ichthyosis and
CC       palmoplantar keratoderma. {ECO:0000269|PubMed:15968592}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   EMBL; AF115436; AAD11436.1; -; mRNA.
DR   EMBL; AF278704; AAF91421.1; -; Genomic_DNA.
DR   EMBL; CR456582; CAG30468.1; -; mRNA.
DR   EMBL; BT007357; AAP36021.1; -; mRNA.
DR   EMBL; BC009715; AAH09715.1; -; mRNA.
DR   CCDS; CCDS13784.1; -.
DR   RefSeq; NP_004773.1; NM_004782.3.
DR   PDB; 4WY4; X-ray; 1.40 A; C=39-116, D=194-258.
DR   PDB; 7BV6; X-ray; 3.05 A; C/G/K/O/S/W=40-130, D/H/L/P/T/X=191-258.
DR   PDBsum; 4WY4; -.
DR   PDBsum; 7BV6; -.
DR   AlphaFoldDB; O95721; -.
DR   SMR; O95721; -.
DR   BioGRID; 114748; 247.
DR   CORUM; O95721; -.
DR   DIP; DIP-56475N; -.
DR   IntAct; O95721; 110.
DR   MINT; O95721; -.
DR   STRING; 9606.ENSP00000215730; -.
DR   GlyCosmos; O95721; 4 sites, 1 glycan.
DR   GlyGen; O95721; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; O95721; -.
DR   MetOSite; O95721; -.
DR   PhosphoSitePlus; O95721; -.
DR   BioMuta; SNAP29; -.
DR   EPD; O95721; -.
DR   jPOST; O95721; -.
DR   MassIVE; O95721; -.
DR   MaxQB; O95721; -.
DR   PaxDb; O95721; -.
DR   PeptideAtlas; O95721; -.
DR   ProteomicsDB; 51014; -.
DR   Antibodypedia; 23352; 213 antibodies from 29 providers.
DR   DNASU; 9342; -.
DR   Ensembl; ENST00000215730.12; ENSP00000215730.6; ENSG00000099940.12.
DR   GeneID; 9342; -.
DR   KEGG; hsa:9342; -.
DR   MANE-Select; ENST00000215730.12; ENSP00000215730.6; NM_004782.4; NP_004773.1.
DR   UCSC; uc011ahw.3; human.
DR   AGR; HGNC:11133; -.
DR   CTD; 9342; -.
DR   DisGeNET; 9342; -.
DR   GeneCards; SNAP29; -.
DR   HGNC; HGNC:11133; SNAP29.
DR   HPA; ENSG00000099940; Low tissue specificity.
DR   MalaCards; SNAP29; -.
DR   MIM; 604202; gene.
DR   MIM; 609528; phenotype.
DR   neXtProt; NX_O95721; -.
DR   OpenTargets; ENSG00000099940; -.
DR   Orphanet; 66631; CEDNIK syndrome.
DR   PharmGKB; PA35981; -.
DR   VEuPathDB; HostDB:ENSG00000099940; -.
DR   eggNOG; KOG3065; Eukaryota.
DR   GeneTree; ENSGT00950000182843; -.
DR   InParanoid; O95721; -.
DR   OMA; NLDEMCD; -.
DR   OrthoDB; 4213488at2759; -.
DR   PhylomeDB; O95721; -.
DR   TreeFam; TF320226; -.
DR   PathwayCommons; O95721; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   SignaLink; O95721; -.
DR   BioGRID-ORCS; 9342; 64 hits in 1166 CRISPR screens.
DR   ChiTaRS; SNAP29; human.
DR   GeneWiki; SNAP29; -.
DR   GenomeRNAi; 9342; -.
DR   Pharos; O95721; Tbio.
DR   PRO; PR:O95721; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; O95721; protein.
DR   Bgee; ENSG00000099940; Expressed in left testis and 204 other tissues.
DR   ExpressionAtlas; O95721; baseline and differential.
DR   Genevisible; O95721; HS.
DR   GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0020018; C:ciliary pocket membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR   GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR   GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR   CDD; cd15856; SNARE_SNAP29C; 1.
DR   CDD; cd15887; SNARE_SNAP29N; 1.
DR   Gene3D; 1.20.5.110; -; 2.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR19305:SF9; SYNAPTOSOMAL-ASSOCIATED PROTEIN 29; 1.
DR   SMART; SM00397; t_SNARE; 2.
DR   SUPFAM; SSF58038; SNARE fusion complex; 2.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Golgi apparatus; Ichthyosis; Membrane; Neuropathy;
KW   Palmoplantar keratoderma; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..258
FT                   /note="Synaptosomal-associated protein 29"
FT                   /id="PRO_0000213601"
FT   DOMAIN          196..258
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..107
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        10..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         130
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   HELIX           40..113
FT                   /evidence="ECO:0007829|PDB:4WY4"
FT   HELIX           195..255
FT                   /evidence="ECO:0007829|PDB:4WY4"
SQ   SEQUENCE   258 AA;  28970 MW;  7E1CDBA22D6F5A3C CRC64;
     MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
     SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
     NYFKSKPVET PPEQNGTLTS QPNNRLKEAI STSKEQEAKY QASHPNLRKL DDTDPVPRGA
     GSAMSTDAYP KNPHLRAYHQ KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
     VDKLDVNIKS TERKVRQL
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