ID A0A3Q7RYH3_VULVU Unreviewed; 1574 AA.
AC A0A3Q7RYH3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 2 isoform X3 {ECO:0000313|RefSeq:XP_025850594.1};
GN Name=RIMS2 {ECO:0000313|RefSeq:XP_025850594.1};
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_025850594.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025850594.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025850594.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025850594.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025850594.1; XM_025994809.1.
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; IPR041282; FYVE_2.
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:SF15; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 26..154
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 86..142
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 637..723
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 774..897
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1420..1538
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 189..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..85
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1574 AA; 177952 MW; 49177DE445615A7F CRC64;
MSAPVGPRGR PAPTPAASQP PLQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKK
LHQQFEMYKE QVKKMGEESQ QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG
GRVSLRSNKV MWVCNLCRKQ QEILTKSGAW FYNSGSNTSQ QPDQKILRGL RNEEAPQEKK
AKVLEQAQFQ GPSGDLSVPA VEKSRSHGLT RQDSIKNGSG VKHQIASDIA SDRTRSPSIS
RDQNRRYDQR EEREEYSQYA TSDNAMPRSP SDYADRRSQR EPQFYEESDH INYRDSNRRS
HRHSKEYIVD DEDVDSRDEY ERQRREEEYQ ARYRSDPNLA RYPVKPQPYE EQMRIHAEVS
RARHERRHSD VSLANAELED SRISMLRMER PSRQRSISER RAAMENQRSY SMERTREAQG
PSSYPQRTTN HSPPTPRRSP IPIDRPDMRR TDSLRKQHHL DPSSAVRKTK REKMETMLRN
DSLSSDQSES VRPPPPKPHK SKKGGKMRQV SLSSSEEELA STPEYTSCDD VEIESESVSE
KGDSQKGKRK TSEQAVLSDS NTRSERQKKM MYFGGHSLEE DLEWSEPQIK DSGVDTCSST
TLNEEHSHSD KHPVTWQPSK DGDRLIGRIL LNKRLKDGSV PRDSGAMLGL KVVGGKMTES
GRLCAFITKV KKGSLADTVG HLRPGDEVLE WNGRLLQGAT FEEVYNIILE SKPEPQVELV
VSRPIGDIPR IPDSTHAQLE SSSSSFESQK MDRPSISVTS PMSPGMLRDV PQYLSGQLSI
KLWFDKVGHQ LIVTILGAKD LPSREDGRPR NPYVKIYFLP DRSDKNKRRT KTVKKTLEPK
WNQTFIYSPV HRREFRERML EITLWDQARV REEESEFLGE ILIELETALL DDEPHWYKLQ
THDVSSLPLP HPSPYMPRRQ LHGESPTRRL QRSKRISDSE ISDYDCDDGI GIVSDYRHNG
RDLQSSTLSV PEQVMSSNHC SPSGSPHRVD VIGRTRSWSP SVPPPQSRNV EQGLRGTRST
AGHYNTISRM DRHRVMDDHY SPDRDSHFLT LPRSRYSQNI EHHHRDGRDC EAADRQPYHR
SRSTEQRPLL ERTTTRSRST ERPDTNLMRS MPSLMTGRSA PPSPALSRSH PRTGSVQTSP
SSTPVAGRRG RQLPQLPPKG TLERSAMDIE ERNRQMKINK YKQVAGSDPR LEQDYHSKYR
SGWDPHRGAD NISTKSSDSD VSDISAVSRT SSASRFSSTS YMSVQSERPR GNKKISVFTS
KMQSRQMGVS GKNMAKSTSI SGDMCSLEKT DGSQSDTAVG ALGTSGKKRR SSIGAKMVAI
VGLSRKSRSA SQLSQTEAGG KKLRSTVQRS TETGLAVEMR NWMTRQASRE STDGSMNSYS
SEGNLIFPGV RLASDSQFSD FLDGLGPAQL VGRQTLATPA MGDIQVGMMD KKGQLEVEII
RARGLVVKPG SKTLPAPYVK VYLLDNGVCI AKKKTKVARK TLEPLYQQLL SFEESPQGKV
LQIIVWGDYG RMDHKSFMGV AQILLDELEL SNMVIGWFKL FPPSSLVDPT LAPLTRRASQ
SSLESSTGPS YSRS
//
