ID A0A3Q7SWX7_VULVU Unreviewed; 1619 AA.
AC A0A3Q7SWX7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=LOW QUALITY PROTEIN: regulating synaptic membrane exocytosis protein 1 {ECO:0000313|RefSeq:XP_025846930.1};
GN Name=RIMS1 {ECO:0000313|RefSeq:XP_025846930.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025846930.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025846930.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025846930.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025846930.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_025846930.1; XM_025991145.1.
DR STRING; 9627.ENSVVUP00000013189; -.
DR KEGG; vvp:112914118; -.
DR OrthoDB; 2891597at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd04031; C2A_RIM1alpha; 1.
DR CDD; cd04028; C2B_RIM1alpha; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR PANTHER; PTHR12157:SF18; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 22..182
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 110..170
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 597..683
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 734..857
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1465..1583
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 180619 MW; C2FA0DEC090ABDAF CRC64;
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MAKPAACKTP RNAENQPHQP SPRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICH
KTKFADGCGH LCSYCRTKFC ARCGGRVSLR SNNEDKVVMW VCNLCRKQQE ILTKSGAWFF
GSGPQQPSQD GTLSDTATGA GSEVPREKKA RLQERSRSQT PLSTAAASSQ DTAPPSAQPD
RSKGAESSQQ AVGPEQKQVS SRSRSEPPRE RKKTAGLSEQ NGKGAQKSER KRVPKSSVQP
GEGAVEDRER KERRESRRLE KGRSQDFPDV PEKREDRKAA EEEKQRKEEE YQTRYRSDPN
LARYPVKPPP EEQQMRMHAR VSRARHERRH SDVAXARXSK AGKRAPAAAR ASPPESPRAY
SAERTAEARA PGAKQLTNHS PPAPRHGPVP AEALEPKAQE PLRKQSRLDP SSAVLIRKSK
REKVETMLRN DSLSSDQSES VRPSPPKPHR SKRGGKKRQM SVSSSEEEGV STPEYTSCED
VELESESVSE KGDLDYYWLD PATWHSRETS PISSHPVTWQ PSKEGDRLIG RVILNKRTTM
PKESGALLGL KVVGGKMTDL GRLGAFITKV KKGSLADVVG HLRAGDEVLE WNGKPLPGAT
NEEVYNIILE SKSEPQVEII VSRPIGDIPR IPESSHPPLE SSSSSFESQK MERPSISVIS
PTSPGALKDA PQVLPGQLSV KLWYDKVGHQ LIVNVLQATD LPTRVDGRPR NPYVKMYFLP
DRSDKSKRRT KTVKKVLEPK WNQTFVYSHV HRRDFRERML EITVWDQPRV QEEESEFLGE
ILIELETALL DDEPHWYKLQ THDESSLPLP QPSPFMPRRH IHGESSSKKL QRSQRISDSD
ISDYEVDDGI GVVPPGYRSS ARESKSTTLT VPEQQRTTHH RSRSVSPHRG DDQGRPRSRL
PNVPLQRSLD EIHPTRRSRS PTRHHDASRS PVDHRSRDVD SQYLSEQDSE LLMLPRAKRG
RSAECLHTTS ELQPSLDRAR SASTNCLRPD TSLHSPERER GRWSPSLDRR RPPSPRIQIQ
HASPENDRHS RKSDRSSIQK QTRKGTASDA ERVLPPCLSR RGYAALRATD QPVLRGKHPA
RSRSSEHSSV RALCSTHHLA PGGSAPPSPL LTRMHRQASP THPPPSDTSF SSRRGRQLPQ
VPVRSGSIEQ ASLVVEERTR QMKMKVHRFK QTTGSGSSQE LDREQYSKYS IHKDQYRSCD
NVSAKSSDSD VSDVSAISRT SSASRLSSTS FMSEQSEHPR GRISSFTPKM QGRRMGTSGR
AITKSTSVSG EMYTLEHNDG SQSDTAVGTV GAGGKKRRSS LSAKVVAIVS RRSRSTSQLS
QTESGHKKLK STIQRSTETG MAAEMRKMVR QPSRESTDGS INSYSSEGNL IFPGVRLGAD
SQFSDFLDGL GPAQLVGRQT LATPAMGDIQ IGMEDKKGQL EVEVIRARSL TQKPGSKSTP
APYVKVYLLE NGACIAKKKT RIARKTLDPL YQQSLVFDES PQGKVLQVIV WGDYGRMDHK
CFMGVAQILL EELDLSSMVI GWYKLFPPSS LVDPTLTPLT RRASQSSLES STGPPCIRS
//
