SYTL4_RAT
ID SYTL4_RAT Reviewed; 672 AA.
AC Q8VHQ7; Q8VHQ6;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Synaptotagmin-like protein 4;
DE AltName: Full=Exophilin-2;
DE AltName: Full=Granuphilin;
GN Name=Sytl4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF VAL-21 AND
RP LEU-43, INTERACTION WITH RAB3A AND STXBP1, AND SUBCELLULAR LOCATION.
RC TISSUE=Insulinoma;
RX PubMed=12058058; DOI=10.1091/mbc.02-02-0025;
RA Coppola T., Frantz C., Perret-Menoud V., Gattesco S., Hirling H.,
RA Regazzi R.;
RT "Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and
RT controls exocytosis.";
RL Mol. Biol. Cell 13:1906-1915(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217 AND SER-274, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12058058};
CC Peripheral membrane protein {ECO:0000269|PubMed:12058058}. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12058058};
CC Peripheral membrane protein {ECO:0000269|PubMed:12058058}.
CC Note=Detected close to the plasma membrane and on secretory granules.
CC In pancreas, interacts with insulin-containing vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Granuphilin-a;
CC IsoId=Q8VHQ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Granuphilin-b;
CC IsoId=Q8VHQ7-2; Sequence=VSP_007903, VSP_007904;
CC -!- TISSUE SPECIFICITY: Detected in insulin-secreting cell lines.
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DR EMBL; AF419341; AAL38513.1; -; mRNA.
DR EMBL; AF419342; AAL38514.1; -; mRNA.
DR RefSeq; NP_536335.1; NM_080410.1. [Q8VHQ7-1]
DR AlphaFoldDB; Q8VHQ7; -.
DR SMR; Q8VHQ7; -.
DR BioGRID; 250808; 2.
DR IntAct; Q8VHQ7; 1.
DR STRING; 10116.ENSRNOP00000004909; -.
DR CarbonylDB; Q8VHQ7; -.
DR iPTMnet; Q8VHQ7; -.
DR PhosphoSitePlus; Q8VHQ7; -.
DR jPOST; Q8VHQ7; -.
DR PaxDb; Q8VHQ7; -.
DR GeneID; 140594; -.
DR KEGG; rno:140594; -.
DR UCSC; RGD:620204; rat. [Q8VHQ7-1]
DR CTD; 94121; -.
DR RGD; 620204; Sytl4.
DR eggNOG; KOG1028; Eukaryota.
DR InParanoid; Q8VHQ7; -.
DR OrthoDB; 916843at2759; -.
DR PhylomeDB; Q8VHQ7; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:Q8VHQ7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
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:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0032418; P:lysosome localization; ISO:RGD.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:RGD.
DR GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:1905684; P:regulation of plasma membrane repair; ISO:RGD.
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; 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 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 Alternative splicing; Cytoplasmic vesicle; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..672
FT /note="Synaptotagmin-like protein 4"
FT /id="PRO_0000190218"
FT DOMAIN 4..122
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 357..479
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 508..634
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 63..105
FT /note="FYVE-type"
FT REGION 199..222
FT /note="Disordered"
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:0000250|UniProtKB:Q96C24"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C24"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C24"
FT VAR_SEQ 485..501
FT /note="ISTESSPGLPAHKGELV -> GSVVAKWWTGWIRLVKK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12058058"
FT /id="VSP_007903"
FT VAR_SEQ 502..672
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12058058"
FT /id="VSP_007904"
FT MUTAGEN 21
FT /note="V->A: Strongly reduces interaction with RAB3A and
FT modulation of exocytosis."
FT /evidence="ECO:0000269|PubMed:12058058"
FT MUTAGEN 43
FT /note="L->A: Strongly reduces interaction with RAB3A and
FT modulation of exocytosis."
FT /evidence="ECO:0000269|PubMed:12058058"
SQ SEQUENCE 672 AA; 75900 MW; 0F994F4D85202400 CRC64;
MSEILDLSFL SEMERDLILS VLQRDEELRK ADEKRIRRLK NELLEIKRKG AKRGSQHYSD
RTCARCQEGL GRLISKSNTC VGCNHLVCRE CRVLESNGSW RCKVCSKEIE LKKATGDWFY
DQKVNRFAYR TGSDIIRMSL RRKPAVNKRE TVGQSLLQQT QMGDIWPGRR IIQEQQKEQS
VLFEVPKLKS GKSALEAESE SLDSYTADSD STSRRDSLDK SGLFPEWKKM SAPKSQVEKE
IAPGNQNAVC GDEGDMIFKK NTRKVLRPSE YTKSVIDLRP EDVAQESGIL GDRSKSVPGL
SVDMEDEEEE EEDIDHLVKL HRQKLARGSM QSGSSMSTIG SMMSLYSEAG DFGNVSVTGK
IAFSLKFEQK TQTLVIHVKE CHQLAYADEA KKRSNPYVKT YLLPDKSRQG KRKTSIKRDT
INPLYDETFR YEISESLLAQ RTLQFSVWHH GRFGRNTFLG EAEVHMDSWK LDKKLDHCLP
LHGKISTESS PGLPAHKGEL VVSLKYIPAS KLPVGGDRKK SKGGEGGELQ VWIKEAKNLT
AAKSGGTSDS FVKGYLLPMR NKASKRKTPV MKKTLNPHYN HTFVYNGVRL EDLQHMCLEL
TVWDREPLAS NDFLGGVRLG VGTGISSGEV VDWMDSTGEE VSLWQKMRQY PGSWAEGTLQ
LRSSMVKQKL GV
