SYT15_HUMAN
ID SYT15_HUMAN Reviewed; 421 AA.
AC Q9BQS2; A5D6W8; Q5VY53; Q5VY55; Q7Z439; Q7Z440;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Synaptotagmin-15;
DE AltName: Full=Chr10Syt;
DE AltName: Full=Synaptotagmin XV;
DE Short=SytXV;
GN Name=SYT15;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RX PubMed=12788067; DOI=10.1016/s0006-291x(03)00911-2;
RA Fukuda M.;
RT "Molecular cloning and characterization of human, rat, and mouse
RT synaptotagmin XV.";
RL Biochem. Biophys. Res. Commun. 306:64-71(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Cerebellum, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 211-374 (ISOFORMS 1/2/3/4).
RC TISSUE=Brain;
RX PubMed=11543631; DOI=10.1006/geno.2001.6619;
RA Craxton M.A.;
RT "Genomic analysis of synaptotagmin genes.";
RL Genomics 77:43-49(2001).
CC -!- FUNCTION: May be involved in the trafficking and exocytosis of
CC secretory vesicles in non-neuronal tissues. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BQS2-2; O15342: ATP6V0E1; NbExp=3; IntAct=EBI-13373352, EBI-12935759;
CC Q9BQS2-2; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-13373352, EBI-11749983;
CC Q9BQS2-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-13373352, EBI-18304435;
CC Q9BQS2-2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-13373352, EBI-13345167;
CC Q9BQS2-2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-13373352, EBI-11721746;
CC Q9BQS2-2; P42858: HTT; NbExp=3; IntAct=EBI-13373352, EBI-466029;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250}; Single-
CC pass type III membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250}; Single-
CC pass type III membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single-
CC pass type III membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Syt XV-a;
CC IsoId=Q9BQS2-1; Sequence=Displayed;
CC Name=2; Synonyms=Syt XV-b;
CC IsoId=Q9BQS2-2; Sequence=VSP_008646;
CC Name=3;
CC IsoId=Q9BQS2-3; Sequence=VSP_008643;
CC Name=4;
CC IsoId=Q9BQS2-4; Sequence=VSP_008644, VSP_008645;
CC -!- DOMAIN: Neither C2 domains mediates Ca(2+)-dependent or -independent
CC phospholipid binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB109022; BAC76817.1; -; mRNA.
DR EMBL; AB109023; BAC76818.1; -; mRNA.
DR EMBL; AK127436; BAC86979.1; -; mRNA.
DR EMBL; AK131036; BAC85479.1; -; mRNA.
DR EMBL; AL356056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139914; AAI39915.1; -; mRNA.
DR EMBL; AJ303363; CAC33885.1; -; mRNA.
DR CCDS; CCDS73103.1; -. [Q9BQS2-1]
DR CCDS; CCDS73104.1; -. [Q9BQS2-2]
DR RefSeq; NP_114118.2; NM_031912.4. [Q9BQS2-1]
DR RefSeq; NP_852660.1; NM_181519.2. [Q9BQS2-2]
DR RefSeq; XP_006718074.1; XM_006718011.1. [Q9BQS2-2]
DR RefSeq; XP_006718160.1; XM_006718097.3. [Q9BQS2-2]
DR RefSeq; XP_016872240.1; XM_017016751.1. [Q9BQS2-2]
DR RefSeq; XP_016872241.1; XM_017016752.1. [Q9BQS2-2]
DR RefSeq; XP_016872510.1; XM_017017021.1.
DR RefSeq; XP_016872512.1; XM_017017023.1. [Q9BQS2-2]
DR AlphaFoldDB; Q9BQS2; -.
DR SMR; Q9BQS2; -.
DR BioGRID; 123765; 9.
DR BioGRID; 3195599; 5.
DR IntAct; Q9BQS2; 7.
DR MINT; Q9BQS2; -.
DR STRING; 9606.ENSP00000363441; -.
DR iPTMnet; Q9BQS2; -.
DR PhosphoSitePlus; Q9BQS2; -.
DR BioMuta; SYT15; -.
DR DMDM; 317373506; -.
DR MassIVE; Q9BQS2; -.
DR MaxQB; Q9BQS2; -.
DR PaxDb; Q9BQS2; -.
DR PeptideAtlas; Q9BQS2; -.
DR PRIDE; Q9BQS2; -.
DR ProteomicsDB; 78711; -. [Q9BQS2-1]
DR ProteomicsDB; 78712; -. [Q9BQS2-2]
DR ProteomicsDB; 78713; -. [Q9BQS2-3]
DR ProteomicsDB; 78714; -. [Q9BQS2-4]
DR Antibodypedia; 66340; 19 antibodies from 10 providers.
DR DNASU; 83849; -.
DR Ensembl; ENST00000374321.9; ENSP00000363441.4; ENSG00000204176.14. [Q9BQS2-1]
DR Ensembl; ENST00000503753.5; ENSP00000427607.1; ENSG00000204176.14. [Q9BQS2-2]
DR GeneID; 102724488; -.
DR GeneID; 83849; -.
DR KEGG; hsa:83849; -.
DR MANE-Select; ENST00000374321.9; ENSP00000363441.4; NM_031912.5; NP_114118.2.
DR MANE-Select; ENST00000615923.4; ENSP00000478933.3; NM_001370184.1; NP_001357113.1.
DR UCSC; uc001jea.4; human. [Q9BQS2-1]
DR CTD; 102724488; -.
DR CTD; 83849; -.
DR GeneCards; SYT15; -.
DR HGNC; HGNC:17167; SYT15.
DR HPA; ENSG00000204176; Low tissue specificity.
DR MIM; 608081; gene.
DR neXtProt; NX_Q9BQS2; -.
DR OpenTargets; ENSG00000204176; -.
DR OpenTargets; ENSG00000277758; -.
DR PharmGKB; PA134921618; -.
DR VEuPathDB; HostDB:ENSG00000204176; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000160819; -.
DR HOGENOM; CLU_023008_11_1_1; -.
DR InParanoid; Q9BQS2; -.
DR OMA; NKLVIWR; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9BQS2; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q9BQS2; -.
DR SignaLink; Q9BQS2; -.
DR BioGRID-ORCS; 102724488; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 83849; 131 hits in 1072 CRISPR screens.
DR Pharos; Q9BQS2; Tdark.
DR PRO; PR:Q9BQS2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BQS2; protein.
DR Bgee; ENSG00000204176; Expressed in right lung and 98 other tissues.
DR ExpressionAtlas; Q9BQS2; baseline and differential.
DR Genevisible; Q9BQS2; HS.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR030539; SYT15.
DR PANTHER; PTHR10024:SF234; PTHR10024:SF234; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Synaptotagmin-15"
FT /id="PRO_0000183980"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..29
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 147..264
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 278..399
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..71
FT /note="MAEQLALVIGGTIGGLLLLLLIGASCCLWRRFCATLTYEELPGTPAMATTAA
FT SSGQRDRPCQPHARTQLSR -> MGVVLLPHPAPSRREPLAPLAPGTRPGWSPAVSGSS
FT RSALRPSTAGPGPGPGTGWGGTAASGRWVPAPAVHCAAPRAAAGHQQHHGPPLCSPDGA
FT PRRFKRRPGSPAPAAQTGETSLREQPHGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008643"
FT VAR_SEQ 333..348
FT /note="KTSAVLGSINPVYNET -> PGPGLGEESRGSLNLK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008644"
FT VAR_SEQ 349..421
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008645"
FT VAR_SEQ 376..421
FT /note="SQQLGRVVVGPYMYTRGRELEHWDEMLSKPKELVKRWHALCRTTEP -> QA
FT TTVELFLFHLTSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12788067,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008646"
FT CONFLICT 246
FT /note="Q -> R (in Ref. 2; BAC85479)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="E -> D (in Ref. 1; BAC76817/BAC76818 and 2;
FT BAC86979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47375 MW; AD9C6CE0957625B7 CRC64;
MAEQLALVIG GTIGGLLLLL LIGASCCLWR RFCATLTYEE LPGTPAMATT AASSGQRDRP
CQPHARTQLS RPPAVPFVVP PTLQGRDWVP LHSGEWADAP WDPCPASELL PHTSSGGLGD
ACMVGAINPE LYKFPEDKSE TDFPDGCLGR LWFSVEYEQE AERLLVGLIK AQHLQAPSET
CSPLVKLYLL PDERRFLQSK TKRKTSNPQF DEHFIFQVSS KTITQRVLKF SVYHVDRQRK
HQLLGQVLFP LKNETLVGDC RRVIWRDLEA ESLEPPSEFG DLQFCLSYND YLSRLTVVVL
RAKGLRLQED RGIVSVFVKV SLMNHNKFVK CKKTSAVLGS INPVYNETFS FKADATELDT
ASLSLTVVQN MEGDKSQQLG RVVVGPYMYT RGRELEHWDE MLSKPKELVK RWHALCRTTE
P
