SYTL4_HUMAN
ID SYTL4_HUMAN Reviewed; 671 AA.
AC Q96C24; Q5H9J3; Q5JPG8; Q8N9P4; Q9H4R0; Q9H4R1;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Synaptotagmin-like protein 4;
DE AltName: Full=Exophilin-2;
DE AltName: Full=Granuphilin;
GN Name=SYTL4;
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] (ISOFORM 1), AND VARIANT VAL-420.
RC TISSUE=Adrenal gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-420.
RC TISSUE=Endometrium, and Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-420.
RC TISSUE=Uterus;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-217 AND SER-289, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-221; SER-289 AND
RP SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP STRUCTURE BY NMR OF 43-105.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the synaptotagmin-like protein
RT 4.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 352-488.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of a C2 domain from human synaptotagmin-like protein
RT 4.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: Modulates exocytosis of dense-core granules and secretion of
CC hormones in the pancreas and the pituitary. Interacts with vesicles
CC containing negatively charged phospholipids in a Ca(2+)-independent
CC manner (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a ternary complex containing STX1A and RAB27A. Can
CC bind both dominant negative and dominant active mutants of RAB27A.
CC Binds STXBP1, RAB3A, RAB8A and RAB27B. Interacts with MYO5A (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96C24; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-747142, EBI-739624;
CC Q96C24; Q92997: DVL3; NbExp=3; IntAct=EBI-747142, EBI-739789;
CC Q96C24; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-747142, EBI-11977403;
CC Q96C24; P51116: FXR2; NbExp=6; IntAct=EBI-747142, EBI-740459;
CC Q96C24; Q9NP66: HMG20A; NbExp=7; IntAct=EBI-747142, EBI-740641;
CC Q96C24; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-747142, EBI-14069005;
CC Q96C24; P25800: LMO1; NbExp=3; IntAct=EBI-747142, EBI-8639312;
CC Q96C24; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-747142, EBI-1216080;
CC Q96C24; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-747142, EBI-1051317;
CC Q96C24; P31321: PRKAR1B; NbExp=3; IntAct=EBI-747142, EBI-2805516;
CC Q96C24; P51159: RAB27A; NbExp=3; IntAct=EBI-747142, EBI-716881;
CC Q96C24; O95716: RAB3D; NbExp=3; IntAct=EBI-747142, EBI-3386067;
CC Q96C24; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-747142, EBI-1378139;
CC Q96C24; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-747142, EBI-12023934;
CC Q96C24; P61764: STXBP1; NbExp=3; IntAct=EBI-747142, EBI-960169;
CC Q96C24; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-747142, EBI-1644036;
CC Q96C24; O94972: TRIM37; NbExp=3; IntAct=EBI-747142, EBI-741602;
CC Q96C24; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-747142, EBI-725997;
CC Q96C24; O15156: ZBTB7B; NbExp=3; IntAct=EBI-747142, EBI-740434;
CC Q96C24; Q96C00: ZBTB9; NbExp=3; IntAct=EBI-747142, EBI-395708;
CC Q96C24; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-747142, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Detected
CC close to the plasma membrane and on secretory granules. In pancreas,
CC interacts with insulin-containing vesicles (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96C24-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96C24-2; Sequence=VSP_015237, VSP_015238;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {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; AK094110; BAC04287.1; -; mRNA.
DR EMBL; BX537410; CAD97652.1; -; mRNA.
DR EMBL; AL832596; CAI46126.1; -; mRNA.
DR EMBL; BC014913; AAH14913.1; -; mRNA.
DR EMBL; Z73900; CAI42004.1; -; Genomic_DNA.
DR EMBL; AL391688; CAI42004.1; JOINED; Genomic_DNA.
DR EMBL; Z73900; CAI42005.1; -; Genomic_DNA.
DR EMBL; AL391688; CAI42005.1; JOINED; Genomic_DNA.
DR CCDS; CCDS14472.1; -. [Q96C24-1]
DR RefSeq; NP_001123368.1; NM_001129896.2. [Q96C24-1]
DR RefSeq; NP_001167539.1; NM_001174068.1. [Q96C24-1]
DR RefSeq; NP_542775.2; NM_080737.2. [Q96C24-1]
DR RefSeq; XP_005262286.1; XM_005262229.2.
DR RefSeq; XP_011529370.1; XM_011531068.2.
DR RefSeq; XP_016885460.1; XM_017029971.1.
DR PDB; 2CSZ; NMR; -; A=43-105.
DR PDB; 3FDW; X-ray; 2.20 A; A/B=352-488.
DR PDB; 5X6T; NMR; -; A=59-111.
DR PDBsum; 2CSZ; -.
DR PDBsum; 3FDW; -.
DR PDBsum; 5X6T; -.
DR AlphaFoldDB; Q96C24; -.
DR BMRB; Q96C24; -.
DR SMR; Q96C24; -.
DR BioGRID; 125120; 46.
DR IntAct; Q96C24; 36.
DR MINT; Q96C24; -.
DR STRING; 9606.ENSP00000362080; -.
DR TCDB; 9.A.57.1.8; the extended-synaptotagmin (e-syt) family.
DR iPTMnet; Q96C24; -.
DR PhosphoSitePlus; Q96C24; -.
DR BioMuta; SYTL4; -.
DR DMDM; 317373281; -.
DR EPD; Q96C24; -.
DR jPOST; Q96C24; -.
DR MassIVE; Q96C24; -.
DR MaxQB; Q96C24; -.
DR PaxDb; Q96C24; -.
DR PeptideAtlas; Q96C24; -.
DR PRIDE; Q96C24; -.
DR ProteomicsDB; 76152; -. [Q96C24-1]
DR ProteomicsDB; 76153; -. [Q96C24-2]
DR Antibodypedia; 28523; 189 antibodies from 23 providers.
DR DNASU; 94121; -.
DR Ensembl; ENST00000263033.9; ENSP00000263033.5; ENSG00000102362.16. [Q96C24-1]
DR Ensembl; ENST00000276141.10; ENSP00000276141.6; ENSG00000102362.16. [Q96C24-1]
DR Ensembl; ENST00000372981.1; ENSP00000362072.1; ENSG00000102362.16. [Q96C24-2]
DR Ensembl; ENST00000372989.6; ENSP00000362080.1; ENSG00000102362.16. [Q96C24-1]
DR Ensembl; ENST00000685623.1; ENSP00000509693.1; ENSG00000102362.16. [Q96C24-1]
DR GeneID; 94121; -.
DR KEGG; hsa:94121; -.
DR MANE-Select; ENST00000372989.6; ENSP00000362080.1; NM_001370165.1; NP_001357094.1.
DR UCSC; uc004egd.6; human. [Q96C24-1]
DR CTD; 94121; -.
DR DisGeNET; 94121; -.
DR GeneCards; SYTL4; -.
DR HGNC; HGNC:15588; SYTL4.
DR HPA; ENSG00000102362; Tissue enhanced (endometrium, ovary).
DR MIM; 300723; gene.
DR neXtProt; NX_Q96C24; -.
DR OpenTargets; ENSG00000102362; -.
DR PharmGKB; PA37987; -.
DR VEuPathDB; HostDB:ENSG00000102362; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000159060; -.
DR HOGENOM; CLU_002711_5_0_1; -.
DR InParanoid; Q96C24; -.
DR OMA; YIPSAKH; -.
DR OrthoDB; 916843at2759; -.
DR PhylomeDB; Q96C24; -.
DR TreeFam; TF341184; -.
DR PathwayCommons; Q96C24; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q96C24; -.
DR BioGRID-ORCS; 94121; 11 hits in 717 CRISPR screens.
DR ChiTaRS; SYTL4; human.
DR EvolutionaryTrace; Q96C24; -.
DR GeneWiki; SYTL4; -.
DR GenomeRNAi; 94121; -.
DR Pharos; Q96C24; Tbio.
DR PRO; PR:Q96C24; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96C24; protein.
DR Bgee; ENSG00000102362; Expressed in left ovary and 152 other tissues.
DR ExpressionAtlas; Q96C24; baseline and differential.
DR Genevisible; Q96C24; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; IDA:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:1905684; P:regulation of plasma membrane repair; IMP:UniProtKB.
DR CDD; cd04029; C2A_SLP-4_5; 1.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR CDD; cd15764; FYVE_Slp4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR044134; FYVE_Slp4.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR037303; SLP-4/5_C2A.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR InterPro; IPR028694; SYTL4.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45716:SF4; PTHR45716:SF4; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..671
FT /note="Synaptotagmin-like protein 4"
FT /id="PRO_0000190216"
FT DOMAIN 4..122
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 356..478
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 507..633
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 63..105
FT /note="FYVE-type"
FT REGION 199..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0Q1"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 336..657
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015237"
FT VAR_SEQ 658..671
FT /note="LQLRSSMAKQKLGL -> VSSIRSVVTGMLGY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015238"
FT VARIANT 420
FT /note="I -> V (in dbSNP:rs2022039)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_016076"
FT CONFLICT 44
FT /note="L -> P (in Ref. 2; CAI46126)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="T -> A (in Ref. 1; BAC04287)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="V -> A (in Ref. 2; CAI46126)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> G (in Ref. 1; BAC04287)"
FT /evidence="ECO:0000305"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2CSZ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2CSZ"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2CSZ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2CSZ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2CSZ"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2CSZ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2CSZ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5X6T"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5X6T"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:3FDW"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 372..382
FT /evidence="ECO:0007829|PDB:3FDW"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:3FDW"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:3FDW"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:3FDW"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 455..464
FT /evidence="ECO:0007829|PDB:3FDW"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:3FDW"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:3FDW"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:3FDW"
SQ SEQUENCE 671 AA; 76024 MW; 04152119330EAB84 CRC64;
MSELLDLSFL SEEEKDLILS VLQRDEEVRK ADEKRIRRLK NELLEIKRKG AKRGSQHYSD
RTCARCQESL GRLSPKTNTC RGCNHLVCRD CRIQESNGTW RCKVCAKEIE LKKATGDWFY
DQKVNRFAYR TGSEIIRMSL RHKPAVSKRE TVGQSLLHQT QMGDIWPGRK IIQERQKEPS
VLFEVPKLKS GKSALEAESE SLDSFTADSD STSRRDSLDK SGLFPEWKKM SAPKSQVEKE
TQPGGQNVVF VDEGEMIFKK NTRKILRPSE YTKSVIDLRP EDVVHESGSL GDRSKSVPGL
NVDMEEEEEE EDIDHLVKLH RQKLARSSMQ SGSSMSTIGS MMSIYSEAGD FGNIFVTGRI
AFSLKYEQQT QSLVVHVKEC HQLAYADEAK KRSNPYVKTY LLPDKSRQGK RKTSIKRDTI
NPLYDETLRY EIPESLLAQR TLQFSVWHHG RFGRNTFLGE AEIQMDSWKL DKKLDHCLPL
HGKISAESPT GLPSHKGELV VSLKYIPASK TPVGGDRKKS KGGEGGELQV WIKEAKNLTA
AKAGGTSDSF VKGYLLPMRN KASKRKTPVM KKTLNPHYNH TFVYNGVRLE DLQHMCLELT
VWDREPLASN DFLGGVRLGV GTGISNGEVV DWMDSTGEEV SLWQKMRQYP GSWAEGTLQL
RSSMAKQKLG L
