SYT15_MOUSE
ID SYT15_MOUSE Reviewed; 418 AA.
AC Q8C6N3; B2RTF1; Q7TN81; Q7TN82; Q8C999;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Synaptotagmin-15;
DE AltName: Full=Synaptotagmin XV;
DE Short=SytXV;
GN Name=Syt15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in the trafficking and exocytosis of
CC secretory vesicles in non-neuronal tissues.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Syt XV-a;
CC IsoId=Q8C6N3-1; Sequence=Displayed;
CC Name=2; Synonyms=Syt XV-b;
CC IsoId=Q8C6N3-2; Sequence=VSP_008649, VSP_008650;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart,
CC lung, skeletal muscle and testis; not detected in brain, liver and
CC kidney. Isoform 1 is expressed in spleen.
CC {ECO:0000269|PubMed:12788067}.
CC -!- DEVELOPMENTAL STAGE: Detected from 7 dpc.
CC {ECO:0000269|PubMed:12788067}.
CC -!- DOMAIN: Neither C2 domains mediates Ca(2+)-dependent or Ca(2+)-
CC independent phospholipid binding.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB109019; BAC76814.1; -; mRNA.
DR EMBL; AB109020; BAC76815.1; -; mRNA.
DR EMBL; AK054180; BAC35683.1; -; mRNA.
DR EMBL; BC139313; AAI39314.1; -; mRNA.
DR EMBL; BC139314; AAI39315.1; -; mRNA.
DR CCDS; CCDS26934.1; -. [Q8C6N3-1]
DR CCDS; CCDS49444.1; -. [Q8C6N3-2]
DR RefSeq; NP_795905.2; NM_176931.2. [Q8C6N3-2]
DR RefSeq; NP_852682.1; NM_181529.4. [Q8C6N3-1]
DR AlphaFoldDB; Q8C6N3; -.
DR SMR; Q8C6N3; -.
DR STRING; 10090.ENSMUSP00000036755; -.
DR iPTMnet; Q8C6N3; -.
DR PhosphoSitePlus; Q8C6N3; -.
DR MaxQB; Q8C6N3; -.
DR PaxDb; Q8C6N3; -.
DR PRIDE; Q8C6N3; -.
DR ProteomicsDB; 254792; -. [Q8C6N3-1]
DR ProteomicsDB; 254793; -. [Q8C6N3-2]
DR DNASU; 319508; -.
DR Ensembl; ENSMUST00000035351; ENSMUSP00000036755; ENSMUSG00000041479. [Q8C6N3-1]
DR Ensembl; ENSMUST00000119693; ENSMUSP00000113725; ENSMUSG00000041479. [Q8C6N3-2]
DR GeneID; 319508; -.
DR KEGG; mmu:319508; -.
DR UCSC; uc007tam.2; mouse. [Q8C6N3-2]
DR UCSC; uc007tan.2; mouse. [Q8C6N3-1]
DR CTD; 83849; -.
DR MGI; MGI:2442166; Syt15.
DR VEuPathDB; HostDB:ENSMUSG00000041479; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000160819; -.
DR HOGENOM; CLU_023008_11_1_1; -.
DR InParanoid; Q8C6N3; -.
DR OMA; NKLVIWR; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q8C6N3; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 319508; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8C6N3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8C6N3; protein.
DR Bgee; ENSMUSG00000041479; Expressed in pancreas and 39 other tissues.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..418
FT /note="Synaptotagmin-15"
FT /id="PRO_0000183981"
FT TOPO_DOM 1..4
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 144..261
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 275..396
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 372..389
FT /note="KSSPLGRVVVGPYMYTRG -> SKAWGMGSRGHGVGATQL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12788067"
FT /id="VSP_008649"
FT VAR_SEQ 390..418
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12788067"
FT /id="VSP_008650"
FT CONFLICT 210
FT /note="N -> D (in Ref. 1; BAC76815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 47270 MW; FC209EB90AA630EE CRC64;
MAEQLAFLIG GIIGGLLLLI GVSCCLWRRF CATFTYEELP ETSDPATISY FSRKEDRLYQ
YSGTPPGRLP SVPFVVPPSH QGRDWVPLHG GDWAVAPQDP CPVPEHMACT SSAKPGDACE
MGSINPELYK SPEDTSETGF PDGCLGRLWF SVEYQQESER LLVGLIKAQQ LQVPSETCST
LVKLHLLPDE RRFLQSKTKH KICNPQFDEN FIFQVSSKSV TQRVLKFSVY HVNKKRKHQL
LGQVLFPLKN ETLAGDHHRI IWRDLEAKNL EPPSEFGDIQ FCLSYNDYLS RLTVVVLRAK
GLQLQEDRSV VSVFVKVSLM NHNKFVKCKR TSAVLGSVNP VYNETFSFKV DTNELDTASL
SLVVLQTTEG NKSSPLGRVV VGPYMYTRGK ELEHWGEMLR KPKELVKRWH ALCRPTEP
