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 24-JAN-2024, entry version 159. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000028648; -. DR PeptideAtlas; Q9EQT6; -. DR ProteomicsDB; 254617; -. DR Antibodypedia; 42821; 151 antibodies from 29 providers. DR DNASU; 80976; -. DR Ensembl; ENSMUST00000028648.3; ENSMUSP00000028648.3; ENSMUSG00000027220.3. DR GeneID; 80976; -. DR KEGG; mmu:80976; -. DR UCSC; uc008lfn.1; mouse. DR AGR; MGI:1933945; -. 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; DEEGQSC; -. DR OrthoDB; 590187at2759; -. DR PhylomeDB; Q9EQT6; -. DR TreeFam; TF315600; -. DR BioGRID-ORCS; 80976; 3 hits in 79 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 179 other cell types or tissues. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. 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:0019905; F:syntaxin 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; IPI:MGI. DR CDD; cd08407; C2B_Synaptotagmin-13; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR028692; Syt13_C2B. DR PANTHER; PTHR10024; SYNAPTOTAGMIN; 1. DR PANTHER; PTHR10024:SF250; SYNAPTOTAGMIN-13; 1. DR Pfam; PF00168; C2; 2. DR SMART; SM00239; C2; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. DR Genevisible; Q9EQT6; MM. 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 //