SYTL2_HUMAN
ID SYTL2_HUMAN Reviewed; 934 AA.
AC Q9HCH5; B3KRS3; B4DJT5; B4DKW3; B4DQ26; B7SA85; B7ZLX6; B7ZLX7; Q2YDA7;
AC Q6TV07; Q6ZN59; Q6ZVC5; Q8ND34; Q96BJ2; Q9H768; Q9NXM1;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Synaptotagmin-like protein 2;
DE AltName: Full=Breast cancer-associated antigen SGA-72M;
DE AltName: Full=Exophilin-4;
GN Name=SYTL2; Synonyms=KIAA1597, SGA72M, SLP2, SLP2A;
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 [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, INTERACTION WITH RAB27A, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DOMAIN, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP GLU-11 AND ARG-32.
RX PubMed=18812475; DOI=10.1182/blood-2008-02-141069;
RA Menasche G., Menager M.M., Lefebvre J.M., Deutsch E., Athman R.,
RA Lambert N., Mahlaoui N., Court M., Garin J., Fischer A.,
RA de Saint Basile G.;
RT "A newly identified isoform of Slp2a associates with Rab27a in cytotoxic T
RT cells and participates in cytotoxic granule secretion.";
RL Blood 112:5052-5062(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Petroziello J.M., Law C.L., Wahl A.F.;
RT "SGA-72M, a breast cancer-associated antigen.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 7; 9; 11 AND 12),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-538 (ISOFORMS 5/6), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-462 (ISOFORMS 1 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 260-934 (ISOFORM 8).
RC TISSUE=Brain, Colon, Mesenchymal stem cell, Teratocarcinoma, Thalamus,
RC Tongue, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 10).
RC TISSUE=Brain, Lung, Mammary gland, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 697-934.
RC TISSUE=Lymph node;
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 [9]
RP ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION, DOMAIN, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=17182843; DOI=10.1091/mbc.e06-10-0914;
RA Yu M., Kasai K., Nagashima K., Torii S., Yokota-Hashimoto H., Okamoto K.,
RA Takeuchi T., Gomi H., Izumi T.;
RT "Exophilin4/Slp2-a targets glucagon granules to the plasma membrane through
RT unique Ca2+-inhibitory phospholipid-binding activity of the C2A domain.";
RL Mol. Biol. Cell 18:688-696(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M.,
RA Saegusa C., Fukuda M., Griffiths G.M.;
RT "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to
RT secretion from the immunological synapse.";
RL Traffic 9:446-457(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-62, AND INTERACTION WITH
RP RAB27A.
RX PubMed=18940603; DOI=10.1016/j.str.2008.07.015;
RA Chavas L.M., Ihara K., Kawasaki M., Torii S., Uejima T., Kato R., Izumi T.,
RA Wakatsuki S.;
RT "Elucidation of Rab27 recruitment by its effectors: structure of Rab27a
RT bound to Exophilin4/Slp2-a.";
RL Structure 16:1468-1477(2008).
CC -!- FUNCTION: Isoform 1 acts as a RAB27A effector protein and plays a role
CC in cytotoxic granule exocytosis in lymphocytes. It is required for
CC cytotoxic granule docking at the immunologic synapse. Isoform 4 binds
CC phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate
CC (PIP2) and promotes the recruitment of glucagon-containing granules to
CC the cell membrane in pancreatic alpha cells. Binding to PS is inhibited
CC by Ca(2+) while binding to PIP2 is Ca(2+) insensitive.
CC {ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782,
CC ECO:0000269|PubMed:18812475}.
CC -!- SUBUNIT: Monomer. Binds NRXN1. Interacts with RAB27B (By similarity).
CC Binds RAB27A that has been activated by GTP-binding. {ECO:0000250,
CC ECO:0000269|PubMed:18812475, ECO:0000269|PubMed:18940603}.
CC -!- INTERACTION:
CC Q9HCH5; P62136: PPP1CA; NbExp=2; IntAct=EBI-2690103, EBI-357253;
CC Q9HCH5; Q9ERI2: Rab27a; Xeno; NbExp=4; IntAct=EBI-2690103, EBI-398172;
CC Q9HCH5-13; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-14291493, EBI-739832;
CC Q9HCH5-13; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-14291493, EBI-10269566;
CC Q9HCH5-13; O95070: YIF1A; NbExp=3; IntAct=EBI-14291493, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:18812475}. Cell membrane
CC {ECO:0000269|PubMed:18266782, ECO:0000269|PubMed:18812475}.
CC Note=Recruited on vesicular structures in cytotoxic T-lymphocytes (CTL)
CC by RAB27A. {ECO:0000269|PubMed:18812475}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC {ECO:0000269|PubMed:17182843}. Note=In the pancreatic alpha cells
CC distributed in both peripheral and anterior regions. Localizes on the
CC glucagon granules in the cell periphery. {ECO:0000269|PubMed:17182843}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=Hematopoietic form of Slp2a, Slp2a-hem;
CC IsoId=Q9HCH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCH5-2; Sequence=VSP_007885;
CC Name=3;
CC IsoId=Q9HCH5-4; Sequence=VSP_007885, VSP_019004;
CC Name=4;
CC IsoId=Q9HCH5-6; Sequence=VSP_037905, VSP_019004;
CC Name=5;
CC IsoId=Q9HCH5-7; Sequence=VSP_037900;
CC Name=6;
CC IsoId=Q9HCH5-8; Sequence=VSP_037900, VSP_037905;
CC Name=7;
CC IsoId=Q9HCH5-9; Sequence=VSP_037896, VSP_037906;
CC Name=8;
CC IsoId=Q9HCH5-11; Sequence=VSP_037900, VSP_037905, VSP_019004;
CC Name=9;
CC IsoId=Q9HCH5-12; Sequence=VSP_037899;
CC Name=10;
CC IsoId=Q9HCH5-13; Sequence=VSP_037904;
CC Name=11;
CC IsoId=Q9HCH5-14; Sequence=VSP_037902, VSP_037905;
CC Name=12;
CC IsoId=Q9HCH5-15; Sequence=VSP_037901, VSP_019004;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in hematopoietic lineages
CC with a strong expression in CD4 and CD8 T-lymphocytes. It is also
CC widely expressed in nonhematopoietic tissues. Isoform 5 is expressed
CC only in nonhematopoietic tissues. Isoform 4 is expressed in pancreatic
CC alpha cells. {ECO:0000269|PubMed:17182843, ECO:0000269|PubMed:18266782,
CC ECO:0000269|PubMed:18812475}.
CC -!- DOMAIN: The RabBD domain mediates interaction with RAB27A and
CC recruitment on to vesicular structures in cytotoxic T-lymphocytes
CC (CTL).
CC -!- DOMAIN: The C2 1 domain mediates binding to phosphatidylserine (PS) and
CC phosphatidylinositol 4,5-bisphosphate (PIP2) and localization to the
CC cell membrane.
CC -!- PTM: Isoform 1 is highly susceptible to proteolytic degradation and is
CC stabilized by the interaction with RAB27A.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR25619.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90989.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB13423.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13423.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB13423.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAD18516.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU035829; ABV82746.1; -; mRNA.
DR EMBL; AY386362; AAR25619.1; ALT_INIT; mRNA.
DR EMBL; AB046817; BAB13423.1; ALT_SEQ; mRNA.
DR EMBL; AK000170; BAA90989.1; ALT_SEQ; mRNA.
DR EMBL; AK024872; BAB15030.1; -; mRNA.
DR EMBL; AK074737; BAC11170.1; -; mRNA.
DR EMBL; AK092121; BAG52485.1; -; mRNA.
DR EMBL; AK124754; BAC85937.1; -; mRNA.
DR EMBL; AK127504; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK131365; BAD18516.1; ALT_INIT; mRNA.
DR EMBL; AK296224; BAG58947.1; -; mRNA.
DR EMBL; AK296740; BAG59325.1; -; mRNA.
DR EMBL; AK298604; BAG60788.1; -; mRNA.
DR EMBL; AP000642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW75110.1; -; Genomic_DNA.
DR EMBL; BC015540; AAH15540.2; -; mRNA.
DR EMBL; BC110315; AAI10316.1; -; mRNA.
DR EMBL; BC136450; AAI36451.1; -; mRNA.
DR EMBL; BC144114; AAI44115.1; -; mRNA.
DR EMBL; BC144115; AAI44116.1; -; mRNA.
DR EMBL; AL834422; CAD39083.1; -; mRNA.
DR CCDS; CCDS31649.1; -. [Q9HCH5-6]
DR CCDS; CCDS31652.1; -. [Q9HCH5-2]
DR CCDS; CCDS41698.1; -. [Q9HCH5-9]
DR CCDS; CCDS53687.1; -. [Q9HCH5-4]
DR CCDS; CCDS53688.1; -. [Q9HCH5-1]
DR CCDS; CCDS53689.1; -. [Q9HCH5-13]
DR CCDS; CCDS76461.1; -. [Q9HCH5-14]
DR RefSeq; NP_001156423.1; NM_001162951.2. [Q9HCH5-1]
DR RefSeq; NP_001156424.1; NM_001162952.2. [Q9HCH5-4]
DR RefSeq; NP_001156425.1; NM_001162953.2. [Q9HCH5-13]
DR RefSeq; NP_001276537.1; NM_001289608.1. [Q9HCH5-14]
DR RefSeq; NP_001276538.1; NM_001289609.1.
DR RefSeq; NP_001276539.1; NM_001289610.1. [Q9HCH5-4]
DR RefSeq; NP_116561.1; NM_032943.4. [Q9HCH5-6]
DR RefSeq; NP_996812.1; NM_206929.3. [Q9HCH5-2]
DR RefSeq; NP_996813.1; NM_206930.3. [Q9HCH5-9]
DR RefSeq; XP_005274124.1; XM_005274067.4.
DR RefSeq; XP_011543416.1; XM_011545114.2.
DR PDB; 3BC1; X-ray; 1.80 A; B/F=10-62.
DR PDB; 7OPP; X-ray; 2.32 A; A/C=5-32.
DR PDB; 7OPQ; X-ray; 2.23 A; A/B=5-32.
DR PDB; 7OPR; X-ray; 2.32 A; A/B=5-32.
DR PDBsum; 3BC1; -.
DR PDBsum; 7OPP; -.
DR PDBsum; 7OPQ; -.
DR PDBsum; 7OPR; -.
DR AlphaFoldDB; Q9HCH5; -.
DR SMR; Q9HCH5; -.
DR BioGRID; 120194; 14.
DR ELM; Q9HCH5; -.
DR IntAct; Q9HCH5; 10.
DR MINT; Q9HCH5; -.
DR STRING; 9606.ENSP00000318803; -.
DR TCDB; 9.A.57.1.4; the extended-synaptotagmin (e-syt) family.
DR GlyGen; Q9HCH5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCH5; -.
DR PhosphoSitePlus; Q9HCH5; -.
DR BioMuta; SYTL2; -.
DR DMDM; 257051068; -.
DR EPD; Q9HCH5; -.
DR jPOST; Q9HCH5; -.
DR MassIVE; Q9HCH5; -.
DR MaxQB; Q9HCH5; -.
DR PaxDb; Q9HCH5; -.
DR PeptideAtlas; Q9HCH5; -.
DR PRIDE; Q9HCH5; -.
DR ProteomicsDB; 81718; -. [Q9HCH5-1]
DR ProteomicsDB; 81719; -. [Q9HCH5-11]
DR ProteomicsDB; 81720; -. [Q9HCH5-12]
DR ProteomicsDB; 81721; -. [Q9HCH5-13]
DR ProteomicsDB; 81722; -. [Q9HCH5-14]
DR ProteomicsDB; 81723; -. [Q9HCH5-15]
DR ProteomicsDB; 81724; -. [Q9HCH5-2]
DR ProteomicsDB; 81725; -. [Q9HCH5-4]
DR ProteomicsDB; 81726; -. [Q9HCH5-6]
DR ProteomicsDB; 81727; -. [Q9HCH5-7]
DR ProteomicsDB; 81728; -. [Q9HCH5-8]
DR ProteomicsDB; 81729; -. [Q9HCH5-9]
DR Antibodypedia; 49544; 75 antibodies from 13 providers.
DR DNASU; 54843; -.
DR Ensembl; ENST00000316356.8; ENSP00000318803.4; ENSG00000137501.18. [Q9HCH5-13]
DR Ensembl; ENST00000389958.7; ENSP00000374608.3; ENSG00000137501.18. [Q9HCH5-9]
DR Ensembl; ENST00000389960.8; ENSP00000374610.4; ENSG00000137501.18. [Q9HCH5-6]
DR Ensembl; ENST00000524452.5; ENSP00000435238.1; ENSG00000137501.18. [Q9HCH5-6]
DR Ensembl; ENST00000525702.5; ENSP00000432996.1; ENSG00000137501.18. [Q9HCH5-2]
DR Ensembl; ENST00000527523.5; ENSP00000434010.1; ENSG00000137501.18. [Q9HCH5-14]
DR Ensembl; ENST00000528231.5; ENSP00000431701.1; ENSG00000137501.18. [Q9HCH5-1]
DR Ensembl; ENST00000529581.5; ENSP00000435855.1; ENSG00000137501.18. [Q9HCH5-2]
DR Ensembl; ENST00000533892.5; ENSP00000432144.1; ENSG00000137501.18. [Q9HCH5-4]
DR GeneID; 54843; -.
DR KEGG; hsa:54843; -.
DR UCSC; uc001pav.5; human. [Q9HCH5-1]
DR CTD; 54843; -.
DR DisGeNET; 54843; -.
DR GeneCards; SYTL2; -.
DR HGNC; HGNC:15585; SYTL2.
DR HPA; ENSG00000137501; Tissue enhanced (intestine, stomach).
DR MIM; 612880; gene.
DR neXtProt; NX_Q9HCH5; -.
DR OpenTargets; ENSG00000137501; -.
DR PharmGKB; PA37985; -.
DR VEuPathDB; HostDB:ENSG00000137501; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155843; -.
DR HOGENOM; CLU_002711_2_0_1; -.
DR InParanoid; Q9HCH5; -.
DR OMA; HFCVADE; -.
DR OrthoDB; 916843at2759; -.
DR PhylomeDB; Q9HCH5; -.
DR TreeFam; TF341184; -.
DR PathwayCommons; Q9HCH5; -.
DR SignaLink; Q9HCH5; -.
DR BioGRID-ORCS; 54843; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; SYTL2; human.
DR EvolutionaryTrace; Q9HCH5; -.
DR GeneWiki; SYTL2; -.
DR GenomeRNAi; 54843; -.
DR Pharos; Q9HCH5; Tbio.
DR PRO; PR:Q9HCH5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HCH5; protein.
DR Bgee; ENSG00000137501; Expressed in saphenous vein and 175 other tissues.
DR ExpressionAtlas; Q9HCH5; baseline and differential.
DR Genevisible; Q9HCH5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043567; SYTL1-5_C2B.
DR InterPro; IPR027006; SYTL2.
DR PANTHER; PTHR45716:SF5; PTHR45716:SF5; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Exocytosis;
KW Membrane; Reference proteome; Repeat.
FT CHAIN 1..934
FT /note="Synaptotagmin-like protein 2"
FT /id="PRO_0000190213"
FT DOMAIN 1..57
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 628..753
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 768..897
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 69..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..569
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037896"
FT VAR_SEQ 1..558
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007885"
FT VAR_SEQ 1..487
FT /note="MIDLSFLTEEEQEAIMKVLQRDAALKRAEEERVRHLPEKIKDDQQLKNMSGQ
FT WFYEAKAKRHRDKIHGADIIRASMRKKRPQIAAEQSKDRENGAKESWVNNVNKDAFLPP
FT ELAGVVEEPEEDAAPASPSSSVVNPASSVIDMSQENTRKPNVSPEKRKNPFNSSKLPEG
FT HSSQQTKNEQSKNGRTGLFQTSKEDELSESKEKSTVADTSIQKLEKSKQTLPGLSNGSQ
FT IKAPIPKARKMIYKSTDLNKDDNQSFPRQRTDSLKARGAPRGILKRNSSSSSTDSETLR
FT YNHNFEPKSKIVSPGLTIHERISEKEHSLEDNSSPNSLEPLKHVRFSAVKDELPQSPGL
FT IHGREVGEFSVLESDRLKNGMEDAGDTEEFQSDPKPSQYRKPSLFHQSTSSPYVSKSET
FT HQPMTSGSFPINGLHSHSEVLTARPQSMENSPTINEPKDKSSELTRLESVLPRSPADEL
FT SHCVEPEPSQVPGGSSRDRQQG -> MDEPNAEQVYNPSQFENLRKFWDLEANSNSKDN
FT DKNITTTSQKNSAPFNRQKHKEFSDIKLSGKNTHEAEVLLSPKKVMAREEMEKLNSKGI
FT LQVLPDEITFPLSPLRKYTYQLPGNESSKENVEKNTEGIVTPVFKEEKDYSEQEIQESI
FT IKTNVLSKDCKDTFNDSLQKLLSETSTPAIQPSGGKVHGKQVLEPSVSENRTWPQKTDF
FT ADTEEEVKGPEKIINEHVDKTVVHPKVKRNSLTASLDKLLKEATGTSPSPLQAKLAPVI
FT TGTNSKLEEGRFFGKGIEQSHNTSADKREILAPFPVRDETFGNTALLKKAESGECQLST
FT QNLIQMAAEDSHPLDPTSQLSRKGSFGDVASPPQDMLFPQDAHLVPQARVHPSQTEISE
FT TVEKVILPPRPVLNDVSAALQKLCGEVWLSYPAGREVGPGEVNPEFPEAVQPVCSPLNP
FT PGVISPWATMDTIVPDRKDFYSSNVVPDKTHEVGSYLAAQMSPSDQTLSSFASIVAQYG
FT KGLPQEVEEIVRETIVQPKSEFLEFSAGLEKLLKEETETFPSKYESDTGNLSPSKLIGS
FT TEEPRRATSECHPEELKETVEKAEAPLITESAFDAGFEKLLKEITEAPPYQPQVSVREE
FT THEKESSQSEQTRFLGTVPHFYRAASQTSEMKDKSNGLESQVNQCDKMLGGDALVTDLL
FT VDFCGSRSGVEIPRTPQLYVAHEIGTIKTVTPPEDRDSESGVAGGQGTLQEPGFGEASE
FT AISVSRNRQPIPLLMNKENSTKTSKVELTLASPYMKQEKEEEKEGFSESDFSDGNTSSN
FT AESWRNPSS (in isoform 5, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_037900"
FT VAR_SEQ 1..487
FT /note="MIDLSFLTEEEQEAIMKVLQRDAALKRAEEERVRHLPEKIKDDQQLKNMSGQ
FT WFYEAKAKRHRDKIHGADIIRASMRKKRPQIAAEQSKDRENGAKESWVNNVNKDAFLPP
FT ELAGVVEEPEEDAAPASPSSSVVNPASSVIDMSQENTRKPNVSPEKRKNPFNSSKLPEG
FT HSSQQTKNEQSKNGRTGLFQTSKEDELSESKEKSTVADTSIQKLEKSKQTLPGLSNGSQ
FT IKAPIPKARKMIYKSTDLNKDDNQSFPRQRTDSLKARGAPRGILKRNSSSSSTDSETLR
FT YNHNFEPKSKIVSPGLTIHERISEKEHSLEDNSSPNSLEPLKHVRFSAVKDELPQSPGL
FT IHGREVGEFSVLESDRLKNGMEDAGDTEEFQSDPKPSQYRKPSLFHQSTSSPYVSKSET
FT HQPMTSGSFPINGLHSHSEVLTARPQSMENSPTINEPKDKSSELTRLESVLPRSPADEL
FT SHCVEPEPSQVPGGSSRDRQQG -> MLFPQDAHLVPQARVHPSQTEISETVEKVILPP
FT RPVLNDVSAALQKLCGEVWLSYPAGREVGPGEVNPEFPEAVQPVCSPLNPPGVISPWAT
FT MDTIVPDRKDFYSSNVVPDKTHEVGSYLAAQMSPSDQTLSSFASIVAQYGKGLPQEVEE
FT IVRETIVQPKSEFLEFSAGLEKLLKEETETFPSKYESDTGNLSPSKLIGSTEEPRRATS
FT ECHPEELKETVEKAEAPLITESAFDAGFEKLLKEITEAPPYQPQVSVREETHEKESSQS
FT EQTRFLGTVPHFYRAASQTSEMKDKSNGLESQVNQCDKMLGGDALVTDLLVDFCGSRSG
FT VEIPRTPQLYVAHEIGTIKTVTPPEDRDSESGVAGGQGTLQEPGFGEASEAISVSRNRQ
FT PIPLLMNKENSTKTSKVELTLASPYMKQEKEEEKEGFSESDFSDGNTSSNAESWRNPSS
FT (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037899"
FT VAR_SEQ 1..142
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037901"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037902"
FT VAR_SEQ 157
FT /note="K -> KQ (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037904"
FT VAR_SEQ 539
FT /note="V -> DEKPDQKPVTNECVPRI (in isoform 4, isoform 6,
FT isoform 8 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_037905"
FT VAR_SEQ 570
FT /note="E -> M (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037906"
FT VAR_SEQ 571..610
FT /note="Missing (in isoform 3, isoform 4, isoform 8 and
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:10997877,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_019004"
FT MUTAGEN 11
FT /note="E->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:18812475"
FT MUTAGEN 32
FT /note="R->A: Abolishes interaction with RAB27A."
FT /evidence="ECO:0000269|PubMed:18812475"
FT CONFLICT 603
FT /note="S -> P (in Ref. 1; ABV82746)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="A -> V (in Ref. 4; BAD18516)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="K -> M (in Ref. 7; AAI44116)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="I -> V (in Ref. 4; BAB15030)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="A -> V (in Ref. 3; BAB13423)"
FT /evidence="ECO:0000305"
FT HELIX 10..35
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:3BC1"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3BC1"
FT VARIANT Q9HCH5-12:6
FT /note="D -> G (in dbSNP:rs556669)"
FT /evidence="ECO:0000305"
FT /id="VAR_082906"
FT VARIANT Q9HCH5-12:20
FT /note="T -> M (in dbSNP:rs641393)"
FT /evidence="ECO:0000305"
FT /id="VAR_082907"
SQ SEQUENCE 934 AA; 104930 MW; 4531F9CDD02F25DE CRC64;
MIDLSFLTEE EQEAIMKVLQ RDAALKRAEE ERVRHLPEKI KDDQQLKNMS GQWFYEAKAK
RHRDKIHGAD IIRASMRKKR PQIAAEQSKD RENGAKESWV NNVNKDAFLP PELAGVVEEP
EEDAAPASPS SSVVNPASSV IDMSQENTRK PNVSPEKRKN PFNSSKLPEG HSSQQTKNEQ
SKNGRTGLFQ TSKEDELSES KEKSTVADTS IQKLEKSKQT LPGLSNGSQI KAPIPKARKM
IYKSTDLNKD DNQSFPRQRT DSLKARGAPR GILKRNSSSS STDSETLRYN HNFEPKSKIV
SPGLTIHERI SEKEHSLEDN SSPNSLEPLK HVRFSAVKDE LPQSPGLIHG REVGEFSVLE
SDRLKNGMED AGDTEEFQSD PKPSQYRKPS LFHQSTSSPY VSKSETHQPM TSGSFPINGL
HSHSEVLTAR PQSMENSPTI NEPKDKSSEL TRLESVLPRS PADELSHCVE PEPSQVPGGS
SRDRQQGSEE EPSPVLKTLE RSAARKMPSK SLEDISSDSS NQAKVDNQPE ELVRSAEDVS
TVPTQPDNPF SHPDKLKRMS KSVPAFLQDE SDDRETDTAS ESSYQLSRHK KSPSSLTNLS
SSSGMTSLSS VSGSVMSVYS GDFGNLEVKG NIQFAIEYVE SLKELHVFVA QCKDLAAADV
KKQRSDPYVK AYLLPDKGKM GKKKTLVVKK TLNPVYNEIL RYKIEKQILK TQKLNLSIWH
RDTFKRNSFL GEVELDLETW DWDNKQNKQL RWYPLKRKTA PVALEAENRG EMKLALQYVP
EPVPGKKLPT TGEVHIWVKE CLDLPLLRGS HLNSFVKCTI LPDTSRKSRQ KTRAVGKTTN
PIFNHTMVYD GFRPEDLMEA CVELTVWDHY KLTNQFLGGL RIGFGTGKSY GTEVDWMDST
SEEVALWEKM VNSPNTWIEA TLPLRMLLIA KISK
