ID   SYTL5_HUMAN             Reviewed;         730 AA.
AC   Q8TDW5; A2RRF2;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Synaptotagmin-like protein 5;
GN   Name=SYTL5; Synonyms=SLP5;
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), INTERACTION WITH RAB27A, AND
RP   INTERACTION WITH PHOSPHOLIPIDS.
RC   TISSUE=Placenta;
RX   PubMed=12051743; DOI=10.1016/s0006-291x(02)00320-0;
RA   Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT   "Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal
RT   tandem C2 domains.";
RL   Biochem. Biophys. Res. Commun. 293:899-906(2002).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 act as Rab effector protein and play a role in vesicle
CC       trafficking. Binds phospholipids.
CC   -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding, and
CC       possibly also RAB3A and RAB6A.
CC   -!- INTERACTION:
CC       Q8TDW5; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-2939487, EBI-739624;
CC       Q8TDW5; O00194: RAB27B; NbExp=5; IntAct=EBI-2939487, EBI-10179046;
CC       Q8TDW5; Q9BTA9: WAC; NbExp=3; IntAct=EBI-2939487, EBI-749118;
CC       Q8TDW5; Q9ERI2: Rab27a; Xeno; NbExp=2; IntAct=EBI-2939487, EBI-398172;
CC       Q8TDW5; P63011: Rab3a; Xeno; NbExp=2; IntAct=EBI-2939487, EBI-398393;
CC       Q8TDW5; P35279: Rab6a; Xeno; NbExp=2; IntAct=EBI-2939487, EBI-444674;
CC       Q8TDW5-2; P54252: ATXN3; NbExp=3; IntAct=EBI-12243980, EBI-946046;
CC       Q8TDW5-2; Q96PX6: CCDC85A; NbExp=3; IntAct=EBI-12243980, EBI-7257229;
CC       Q8TDW5-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-12243980, EBI-739624;
CC       Q8TDW5-2; P51159: RAB27A; NbExp=3; IntAct=EBI-12243980, EBI-716881;
CC       Q8TDW5-2; O00194: RAB27B; NbExp=3; IntAct=EBI-12243980, EBI-10179046;
CC       Q8TDW5-2; O76024: WFS1; NbExp=3; IntAct=EBI-12243980, EBI-720609;
CC       Q8TDW5-2; O95070: YIF1A; NbExp=3; IntAct=EBI-12243980, EBI-2799703;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TDW5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TDW5-2; Sequence=VSP_042659;
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta and liver.
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DR   EMBL; AB080222; BAB88906.1; -; mRNA.
DR   EMBL; AL121578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC131585; AAI31586.1; -; mRNA.
DR   CCDS; CCDS14244.1; -. [Q8TDW5-1]
DR   CCDS; CCDS55399.1; -. [Q8TDW5-2]
DR   RefSeq; NP_001156806.1; NM_001163334.1. [Q8TDW5-2]
DR   RefSeq; NP_001156807.1; NM_001163335.1. [Q8TDW5-1]
DR   RefSeq; NP_620135.1; NM_138780.2. [Q8TDW5-1]
DR   RefSeq; XP_011542303.1; XM_011544001.2. [Q8TDW5-2]
DR   RefSeq; XP_011542304.1; XM_011544002.2. [Q8TDW5-2]
DR   RefSeq; XP_016885461.1; XM_017029972.1. [Q8TDW5-2]
DR   RefSeq; XP_016885462.1; XM_017029973.1. [Q8TDW5-2]
DR   RefSeq; XP_016885463.1; XM_017029974.1. [Q8TDW5-2]
DR   AlphaFoldDB; Q8TDW5; -.
DR   SMR; Q8TDW5; -.
DR   BioGRID; 125121; 16.
DR   IntAct; Q8TDW5; 12.
DR   STRING; 9606.ENSP00000395220; -.
DR   iPTMnet; Q8TDW5; -.
DR   PhosphoSitePlus; Q8TDW5; -.
DR   BioMuta; SYTL5; -.
DR   DMDM; 33301662; -.
DR   EPD; Q8TDW5; -.
DR   jPOST; Q8TDW5; -.
DR   MassIVE; Q8TDW5; -.
DR   MaxQB; Q8TDW5; -.
DR   PaxDb; 9606-ENSP00000395220; -.
DR   PeptideAtlas; Q8TDW5; -.
DR   ProteomicsDB; 74354; -. [Q8TDW5-1]
DR   ProteomicsDB; 74355; -. [Q8TDW5-2]
DR   Pumba; Q8TDW5; -.
DR   Antibodypedia; 10579; 118 antibodies from 23 providers.
DR   DNASU; 94122; -.
DR   Ensembl; ENST00000297875.7; ENSP00000297875.2; ENSG00000147041.12. [Q8TDW5-1]
DR   Ensembl; ENST00000456733.2; ENSP00000395220.2; ENSG00000147041.12. [Q8TDW5-2]
DR   GeneID; 94122; -.
DR   KEGG; hsa:94122; -.
DR   MANE-Select; ENST00000297875.7; ENSP00000297875.2; NM_138780.3; NP_620135.1.
DR   UCSC; uc004ddv.4; human. [Q8TDW5-1]
DR   AGR; HGNC:15589; -.
DR   CTD; 94122; -.
DR   DisGeNET; 94122; -.
DR   GeneCards; SYTL5; -.
DR   HGNC; HGNC:15589; SYTL5.
DR   HPA; ENSG00000147041; Tissue enhanced (brain, stomach).
DR   neXtProt; NX_Q8TDW5; -.
DR   OpenTargets; ENSG00000147041; -.
DR   PharmGKB; PA37988; -.
DR   VEuPathDB; HostDB:ENSG00000147041; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   GeneTree; ENSGT00940000158618; -.
DR   HOGENOM; CLU_002711_5_0_1; -.
DR   InParanoid; Q8TDW5; -.
DR   OMA; PGTERRW; -.
DR   OrthoDB; 590187at2759; -.
DR   PhylomeDB; Q8TDW5; -.
DR   TreeFam; TF341184; -.
DR   PathwayCommons; Q8TDW5; -.
DR   SignaLink; Q8TDW5; -.
DR   BioGRID-ORCS; 94122; 9 hits in 768 CRISPR screens.
DR   ChiTaRS; SYTL5; human.
DR   GenomeRNAi; 94122; -.
DR   Pharos; Q8TDW5; Tbio.
DR   PRO; PR:Q8TDW5; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q8TDW5; Protein.
DR   Bgee; ENSG00000147041; Expressed in pancreatic ductal cell and 128 other cell types or tissues.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04029; C2A_SLP-4_5; 1.
DR   CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR   CDD; cd15766; FYVE_Slp5; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR041282; FYVE_2.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR037303; SLP-4/5_C2A.
DR   InterPro; IPR043567; SYTL1-5_C2B.
DR   InterPro; IPR042783; SYTL5_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45716; BITESIZE, ISOFORM I; 1.
DR   PANTHER; PTHR45716:SF6; SYNAPTOTAGMIN-LIKE PROTEIN 5; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; FYVE_2; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
DR   Genevisible; Q8TDW5; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..730
FT                   /note="Synaptotagmin-like protein 5"
FT                   /id="PRO_0000190219"
FT   DOMAIN          7..123
FT                   /note="RabBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT   DOMAIN          406..527
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          563..694
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   ZN_FING         64..106
FT                   /note="FYVE-type"
FT   REGION          147..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T23"
FT   VAR_SEQ         384
FT                   /note="S -> STSSQAGSDRKWTYLNVPDADSD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042659"
FT   VARIANT         275
FT                   /note="I -> V (in dbSNP:rs4827331)"
FT                   /id="VAR_024601"
FT   VARIANT         302
FT                   /note="R -> C (in dbSNP:rs57226394)"
FT                   /id="VAR_061753"
SQ   SEQUENCE   730 AA;  81523 MW;  D9E0DA98880A95ED CRC64;
     MSKNSEFINL SFLLDHEKEM ILGVLKRDEY LKKVEDKRIR KLKNELLEAK RRSGKTQQEA
     SRVCVHCHRN LGLIFDRGDP CQACSLRVCR ECRVAGPNGS WKCTVCDKIA QLRIITGEWF
     FEEKAKRFKQ VNVLGTDVVR QSILRRSPGA EEVQSQEQTR QDAEKSDTSP VAGKKASHDG
     PKRKGFLLSK FRSATRGEII TPKTDTGRSY SLDLDGQHFR SLKSPPGSDR GSTGSSDLND
     QEPGPRTPKS SRSNGVTPGT QSSPAPSTRT VTSVISREYG FENSMDLAAI EGTSQELTKS
     HRRNTSGTPS IAVSGTSLSS DQSRSELDLS ESFTEDSEDT VSIRSKSVPG ALDKDSLEET
     EESIDALVSS QLSTNTHRLA SGLSTTSLNS MMSVYSETGD YGNVKVSGEI LLHISYCYKT
     GGLYIFVKNC RNLAIGDEKK QRTDAYVKSY LLPDKSRNNK RKTKIRTGTN PEFNETLKYT
     ISHTQLETRT LQLSVWHYDR FGRNSFLGEV EIPFDSWNFE NPTDEWFVLQ PKVEFAPDIG
     LQYKGELTVV LRYIPPEENL MLPPEQLQGN KTFKKGKKKE SPVISGGILE VFIKEAKNLT
     AVKSGGTSDS FVKGYLLPDD SKATKHKTLV IKKSVNPQWN HTFMFSGIHP QDIKNVCLEL
     TIWDKEAFSS NIFLGGVRLN SGSGVSHGKN VDWMDSQGEE QRLWQKMANN PGTPFEGVLM
     LRSSMGKCRL
//