SYT13_MOUSE
ID SYT13_MOUSE Reviewed; 426 AA.
AC Q9EQT6; Q6ZPR2; Q8BRK6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Synaptotagmin-13;
DE AltName: Full=Synaptotagmin XIII;
DE Short=SytXIII;
GN Name=Syt13; Synonyms=Kiaa1427;
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], INTERACTION WITH NRXN1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=11171101; DOI=10.1042/0264-6021:3540249;
RA Fukuda M., Mikoshiba K.;
RT "Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt
RT XIII).";
RL Biochem. J. 354:249-257(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Hippocampus;
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].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 transport vesicle docking to the plasma
CC membrane.
CC -!- SUBUNIT: Interacts with NRXN1. {ECO:0000269|PubMed:11171101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11171101}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11171101}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, spleen, lung and testis.
CC {ECO:0000269|PubMed:11171101}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 dpc onwards.
CC {ECO:0000269|PubMed:11171101}.
CC -!- DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent
CC phospholipid binding.
CC -!- DOMAIN: The second C2 domain/C2B domain binds phospholipids regardless
CC of whether calcium is present.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB048947; BAB19628.1; -; mRNA.
DR EMBL; AK044038; BAC31748.1; -; mRNA.
DR EMBL; AK049840; BAC33948.1; -; mRNA.
DR EMBL; AK082425; BAC38491.1; -; mRNA.
DR EMBL; AK129357; BAC98167.1; ALT_INIT; mRNA.
DR EMBL; BC030907; AAH30907.1; -; mRNA.
DR CCDS; CCDS16451.1; -.
DR RefSeq; NP_109650.1; NM_030725.4.
DR AlphaFoldDB; Q9EQT6; -.
DR SMR; Q9EQT6; -.
DR STRING; 10090.ENSMUSP00000028648; -.
DR iPTMnet; Q9EQT6; -.
DR PhosphoSitePlus; Q9EQT6; -.
DR SwissPalm; Q9EQT6; -.
DR PaxDb; Q9EQT6; -.
DR PeptideAtlas; Q9EQT6; -.
DR PRIDE; Q9EQT6; -.
DR ProteomicsDB; 254617; -.
DR Antibodypedia; 42821; 137 antibodies from 29 providers.
DR DNASU; 80976; -.
DR Ensembl; ENSMUST00000028648; ENSMUSP00000028648; ENSMUSG00000027220.
DR GeneID; 80976; -.
DR KEGG; mmu:80976; -.
DR UCSC; uc008lfn.1; mouse.
DR CTD; 57586; -.
DR MGI; MGI:1933945; Syt13.
DR VEuPathDB; HostDB:ENSMUSG00000027220; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000160226; -.
DR HOGENOM; CLU_023008_2_0_1; -.
DR InParanoid; Q9EQT6; -.
DR OMA; CDCYIQG; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9EQT6; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 80976; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Syt13; mouse.
DR PRO; PR:Q9EQT6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQT6; protein.
DR Bgee; ENSMUSG00000027220; Expressed in islet of Langerhans and 177 other tissues.
DR Genevisible; Q9EQT6; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
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:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IPI:MGI.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR028692; SYT13.
DR PANTHER; PTHR10024:SF250; PTHR10024:SF250; 1.
DR Pfam; PF00168; C2; 2.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..426
FT /note="Synaptotagmin-13"
FT /id="PRO_0000183976"
FT TOPO_DOM 1..6
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 158..275
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 287..422
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 52
FT /note="R -> G (in Ref. 2; BAC31748)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="E -> G (in Ref. 3; BAC98167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46870 MW; 8B67FAF369861CBE CRC64;
MVLSVPVIAL GATLGTATSI LALCGVTCLC RHMHPKKGLL PRDREPDPEK ARPGVLQAAQ
QFNIKKSTEP VQPRPLLKFP DIYGPRPAVT APEVINYADY TLETTEESAA PASPQAQSDS
RLKRQVTEEL SIRPQNGVVE DVCVMETWNP EKAASWNQAP KLHFRLDYDQ KKAELFVTSL
EAVTSDHEGG CDCYIQGSVA VKTGSVEAQT ALKKRQLHTT WEEGLALPLG EEELPTATLT
LTLRTCDRFS RHSVIGELRL GLDGASVPLG AAQWGELKTT AKEPSAGAGE VLLSISYLPA
ANRLLVVLIK AKNLHSNQSK ELLGKDVSVK VTLKHQAQKL KKKQTKRAKH KINPVWNEMI
MFELPDDLLR ASSVELEVLG QGEEGPSCEL GHCSLGLHAS GSERSHWEEM LKNPRRQIAM
WHQLHL
