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SYT13_HUMAN
ID   SYT13_HUMAN             Reviewed;         426 AA.
AC   Q7L8C5; A8K4P4; D3DQP1; Q9BQS3; Q9H041; Q9P2C0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Synaptotagmin-13;
DE   AltName: Full=Synaptotagmin XIII;
DE            Short=SytXIII;
GN   Name=SYT13; Synonyms=KIAA1427;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 150-322, AND TISSUE SPECIFICITY.
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).
RN   [7]
RP   STRUCTURE BY NMR OF 155-280.
RG   RIKEN structural genomics initiative (RSGI);
RT   "The first C2 domain of human synaptotagmin XIII.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: May be involved in transport vesicle docking to the plasma
CC       membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NRXN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, pancreas and kidney.
CC       {ECO:0000269|PubMed:11543631}.
CC   -!- DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent
CC       phospholipid binding. {ECO:0000250}.
CC   -!- DOMAIN: The second C2 domain/C2B domain binds phospholipids regardless
CC       of whether calcium is present. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB037848; BAA92665.1; ALT_INIT; mRNA.
DR   EMBL; AK291009; BAF83698.1; -; mRNA.
DR   EMBL; AL512743; CAC21669.1; -; mRNA.
DR   EMBL; CH471064; EAW68043.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68044.1; -; Genomic_DNA.
DR   EMBL; BC093830; AAH93830.1; -; mRNA.
DR   EMBL; BC093832; AAH93832.1; -; mRNA.
DR   EMBL; AJ303362; CAC33884.1; -; mRNA.
DR   CCDS; CCDS31470.1; -.
DR   RefSeq; NP_065877.1; NM_020826.2.
DR   PDB; 1WFM; NMR; -; A=155-279.
DR   PDBsum; 1WFM; -.
DR   AlphaFoldDB; Q7L8C5; -.
DR   SMR; Q7L8C5; -.
DR   BioGRID; 121638; 7.
DR   IntAct; Q7L8C5; 1.
DR   STRING; 9606.ENSP00000020926; -.
DR   GlyGen; Q7L8C5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7L8C5; -.
DR   PhosphoSitePlus; Q7L8C5; -.
DR   BioMuta; SYT13; -.
DR   DMDM; 74749900; -.
DR   MassIVE; Q7L8C5; -.
DR   PaxDb; Q7L8C5; -.
DR   PeptideAtlas; Q7L8C5; -.
DR   PRIDE; Q7L8C5; -.
DR   ProteomicsDB; 68836; -.
DR   Antibodypedia; 42821; 137 antibodies from 29 providers.
DR   DNASU; 57586; -.
DR   Ensembl; ENST00000020926.8; ENSP00000020926.3; ENSG00000019505.8.
DR   GeneID; 57586; -.
DR   KEGG; hsa:57586; -.
DR   MANE-Select; ENST00000020926.8; ENSP00000020926.3; NM_020826.3; NP_065877.1.
DR   UCSC; uc001myq.3; human.
DR   CTD; 57586; -.
DR   DisGeNET; 57586; -.
DR   GeneCards; SYT13; -.
DR   HGNC; HGNC:14962; SYT13.
DR   HPA; ENSG00000019505; Tissue enhanced (brain, gallbladder, pituitary gland).
DR   MIM; 607716; gene.
DR   neXtProt; NX_Q7L8C5; -.
DR   OpenTargets; ENSG00000019505; -.
DR   PharmGKB; PA37942; -.
DR   VEuPathDB; HostDB:ENSG00000019505; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   GeneTree; ENSGT00940000160226; -.
DR   HOGENOM; CLU_023008_2_0_1; -.
DR   InParanoid; Q7L8C5; -.
DR   OMA; CDCYIQG; -.
DR   OrthoDB; 925064at2759; -.
DR   PhylomeDB; Q7L8C5; -.
DR   TreeFam; TF315600; -.
DR   PathwayCommons; Q7L8C5; -.
DR   SignaLink; Q7L8C5; -.
DR   BioGRID-ORCS; 57586; 6 hits in 1066 CRISPR screens.
DR   ChiTaRS; SYT13; human.
DR   EvolutionaryTrace; Q7L8C5; -.
DR   GeneWiki; SYT13; -.
DR   GenomeRNAi; 57586; -.
DR   Pharos; Q7L8C5; Tbio.
DR   PRO; PR:Q7L8C5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q7L8C5; protein.
DR   Bgee; ENSG00000019505; Expressed in middle temporal gyrus and 119 other tissues.
DR   ExpressionAtlas; Q7L8C5; baseline and differential.
DR   Genevisible; Q7L8C5; HS.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; IDA:LIFEdb.
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; IBA:GO_Central.
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   3D-structure; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..426
FT                   /note="Synaptotagmin-13"
FT                   /id="PRO_0000183975"
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   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          174..183
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          193..201
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          238..245
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          255..267
FT                   /evidence="ECO:0007829|PDB:1WFM"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:1WFM"
SQ   SEQUENCE   426 AA;  46885 MW;  9BD0AD533E0CE886 CRC64;
     MVLSVPVIAL GATLGTATSI LALCGVTCLC RHMHPKKGLL PRDQDPDLEK AKPSLLGSAQ
     QFNVKKSTEP VQPRALLKFP DIYGPRPAVT APEVINYADY SLRSTEEPTA PASPQPPNDS
     RLKRQVTEEL FILPQNGVVE DVCVMETWNP EKAASWNQAP KLHYCLDYDC QKAELFVTRL
     EAVTSNHDGG CDCYVQGSVA NRTGSVEAQT ALKKRQLHTT WEEGLVLPLA EEELPTATLT
     LTLRTCDRFS RHSVAGELRL GLDGTSVPLG AAQWGELKTS AKEPSAGAGE VLLSISYLPA
     ANRLLVVLIK AKNLHSNQSK ELLGKDVSVK VTLKHQARKL KKKQTKRAKH KINPVWNEMI
     MFELPDDLLQ ASSVELEVLG QDDSGQSCAL GHCSLGLHTS GSERSHWEEM LKNPRRQIAM
     WHQLHL
 
 
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