ID SYT11_HUMAN Reviewed; 431 AA. AC Q9BT88; Q14998; Q5W0D4; Q68CT5; Q8IXU3; Q96SU2; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 09-DEC-2015, entry version 138. DE RecName: Full=Synaptotagmin-11; DE AltName: Full=Synaptotagmin XI; DE Short=SytXI; GN Name=SYT11; Synonyms=KIAA0080; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48. RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [2] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48. RC TISSUE=Amygdala; 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-48 AND RP VAL-231. RC TISSUE=Brain, and Lymph; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH PARK2, UBIQUITINATION, AND SUBCELLULAR LOCATION. RX PubMed=12925569; DOI=10.1093/hmg/ddg269; RA Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M.; RT "The autosomal recessive juvenile Parkinson disease gene product, RT parkin, interacts with and ubiquitinates synaptotagmin XI."; RL Hum. Mol. Genet. 12:2587-2597(2003). CC -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of CC secretory vesicles through Ca(2+) and phospholipid binding to the CC C2 domain or may serve as Ca(2+) sensors in the process of CC vesicular trafficking and exocytosis. {ECO:0000250}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 CC domains. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. Can also form heterodimers (By similarity). CC Interacts with PARK2. {ECO:0000250, ECO:0000269|PubMed:12925569}. CC -!- INTERACTION: CC Q92624:APPBP2; NbExp=3; IntAct=EBI-751770, EBI-743771; CC Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-751770, EBI-6308763; CC O43765:SGTA; NbExp=4; IntAct=EBI-751770, EBI-347996; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12925569}; CC Single-pass membrane protein {ECO:0000269|PubMed:12925569}. Cell CC junction, synapse {ECO:0000250}. Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass CC membrane protein {ECO:0000250}. Note=In substantia nigra, observed CC in neuronal cell bodies and neurites. Found in the core of the CC Lewy bodies in the brain of sporadic Parkinson disease patients. CC -!- PTM: Ubiquitinated and targeted to the proteasome complex for CC degradation. {ECO:0000269|PubMed:12925569}. CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 C2 domains. {ECO:0000255|PROSITE- CC ProRule:PRU00041}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA07527.2; 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; D38522; BAA07527.2; ALT_INIT; mRNA. DR EMBL; AK027540; BAB55186.1; -; mRNA. DR EMBL; AK074931; BAC11300.1; -; mRNA. DR EMBL; CR749792; CAH18653.1; -; mRNA. DR EMBL; AL139128; CAH69948.1; -; Genomic_DNA. DR EMBL; BC004291; AAH04291.1; -; mRNA. DR EMBL; BC013690; AAH13690.1; -; mRNA. DR EMBL; BC039205; AAH39205.1; -; mRNA. DR CCDS; CCDS1122.1; -. DR RefSeq; NP_689493.3; NM_152280.4. DR UniGene; Hs.32984; -. DR ProteinModelPortal; Q9BT88; -. DR SMR; Q9BT88; 158-430. DR BioGrid; 116815; 10. DR IntAct; Q9BT88; 3. DR MINT; MINT-240234; -. DR STRING; 9606.ENSP00000357307; -. DR PhosphoSite; Q9BT88; -. DR BioMuta; SYT11; -. DR DMDM; 215273917; -. DR MaxQB; Q9BT88; -. DR PaxDb; Q9BT88; -. DR PRIDE; Q9BT88; -. DR DNASU; 23208; -. DR Ensembl; ENST00000368324; ENSP00000357307; ENSG00000132718. DR GeneID; 23208; -. DR KEGG; hsa:23208; -. DR UCSC; uc001fmg.3; human. DR CTD; 23208; -. DR GeneCards; SYT11; -. DR H-InvDB; HIX0001138; -. DR HGNC; HGNC:19239; SYT11. DR HPA; HPA064091; -. DR MIM; 608741; gene. DR neXtProt; NX_Q9BT88; -. DR PharmGKB; PA134898675; -. DR eggNOG; KOG1028; Eukaryota. DR eggNOG; ENOG410XRME; LUCA. DR GeneTree; ENSGT00760000118973; -. DR HOGENOM; HOG000232126; -. DR HOVERGEN; HBG005010; -. DR InParanoid; Q9BT88; -. DR OMA; IKVDYGD; -. DR OrthoDB; EOG75J0N2; -. DR PhylomeDB; Q9BT88; -. DR TreeFam; TF315600; -. DR ChiTaRS; SYT11; human. DR GeneWiki; SYT11; -. DR GenomeRNAi; 23208; -. DR NextBio; 44743; -. DR PRO; PR:Q9BT88; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q9BT88; -. DR CleanEx; HS_SYT11; -. DR Genevisible; Q9BT88; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central. DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central. DR GO; GO:0048791; P:calcium ion-dependent exocytosis of neurotransmitter; IBA:GO_Central. DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; TAS:ParkinsonsUK-UCL. DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central. DR Gene3D; 2.60.40.150; -; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR001565; Synaptotagmin. DR InterPro; IPR028699; SYT11. DR PANTHER; PTHR10024:SF115; PTHR10024:SF115; 1. DR Pfam; PF00168; C2; 2. DR PRINTS; PR00399; SYNAPTOTAGMN. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; SSF49562; 2. DR PROSITE; PS50004; C2; 2. PE 1: Evidence at protein level; KW Calcium; Cell junction; Complete proteome; Cytoplasmic vesicle; KW Membrane; Metal-binding; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Synapse; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1 431 Synaptotagmin-11. FT /FTId=PRO_0000183969. FT TOPO_DOM 1 15 Vesicular. {ECO:0000255}. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TOPO_DOM 37 431 Cytoplasmic. {ECO:0000255}. FT DOMAIN 174 262 C2 1. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 304 397 C2 2. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT METAL 188 188 Calcium 1. {ECO:0000250}. FT METAL 188 188 Calcium 2. {ECO:0000250}. FT METAL 195 195 Calcium 1. {ECO:0000250}. FT METAL 249 249 Calcium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 250 250 Calcium 1. {ECO:0000250}. FT METAL 250 250 Calcium 2. {ECO:0000250}. FT METAL 250 250 Calcium 3. {ECO:0000250}. FT METAL 253 253 Calcium 3. {ECO:0000250}. FT METAL 256 256 Calcium 2. {ECO:0000250}. FT METAL 256 256 Calcium 3. {ECO:0000250}. FT MOD_RES 134 134 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9R0N3}. FT VARIANT 48 48 Q -> H (in dbSNP:rs822522). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:7584044}. FT /FTId=VAR_047656. FT VARIANT 231 231 G -> V (in dbSNP:rs17853892). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_047657. FT CONFLICT 50 50 N -> S (in Ref. 3; BAB55186). FT {ECO:0000305}. FT CONFLICT 268 268 V -> A (in Ref. 3; BAB55186). FT {ECO:0000305}. FT CONFLICT 359 359 F -> L (in Ref. 4; CAH18653). FT {ECO:0000305}. FT CONFLICT 370 370 D -> G (in Ref. 4; CAH18653). FT {ECO:0000305}. SQ SEQUENCE 431 AA; 48297 MW; 5C8667D2C23D758E CRC64; MAEITNIRPS FDVSPVVAGL IGASVLVVCV SVTVFVWSCC HQQAEKKQKN PPYKFIHMLK GISIYPETLS NKKKIIKVRR DKDGPGREGG RRNLLVDAAE AGLLSRDKDP RGPSSGSCID QLPIKMDYGE ELRSPITSLT PGESKTTSPS SPEEDVMLGS LTFSVDYNFP KKALVVTIQE AHGLPVMDDQ TQGSDPYIKM TILPDKRHRV KTRVLRKTLD PVFDETFTFY GIPYSQLQDL VLHFLVLSFD RFSRDDVIGE VMVPLAGVDP STGKVQLTRD IIKRNIQKCI SRGELQVSLS YQPVAQRMTV VVLKARHLPK MDITGLSGNP YVKVNVYYGR KRIAKKKTHV KKCTLNPIFN ESFIYDIPTD LLPDISIEFL VIDFDRTTKN EVVGRLILGA HSVTASGAEH WREVCESPRK PVAKWHSLSE Y //