ID A0A3Q7RYJ5_VULVU Unreviewed; 1549 AA.
AC A0A3Q7RYJ5;
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 X27 {ECO:0000313|RefSeq:XP_025850619.1};
GN Name=RIMS2 {ECO:0000313|RefSeq:XP_025850619.1};
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_025850619.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025850619.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025850619.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025850619.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025850619.1; XM_025994834.1.
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 590..676
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 727..850
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1395..1513
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..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1326
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 688..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1549 AA; 175310 MW; C40F483CD94CCC0C 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
KGDMDYNWLD HTSWHSSEAS PMSLHPVTWQ PSKDGDRLIG RILLNKRLKD GSVPRDSGAM
LGLKVVGGKM TESGRLCAFI TKVKKGSLAD TVGHLRPGDE VLEWNGRLLQ GATFEEVYNI
ILESKPEPQV ELVVSRPIGD IPRIPDSTHA QLESSSSSFE SQKMDRPSIS VTSPMSPGML
RDVPQYLSGQ LSIKLWFDKV GHQLIVTILG AKDLPSREDG RPRNPYVKIY FLPDRSDKNK
RRTKTVKKTL EPKWNQTFIY SPVHRREFRE RMLEITLWDQ ARVREEESEF LGEILIELET
ALLDDEPHWY KLQTHDVSSL PLPHPSPYMP RRQLHGESPT RRLQRSKRIS DSEISDYDCD
DGIGIVSDYR HNGRDLQSST LSVPEQVMSS NHCSPSGSPH RVDVIGRTRS WSPSVPPPQS
RNVEQGLRGT RSTAGHYNTI SRMDRHRVMD DHYSPDRDSH FLTLPRSRYS QNIEHHHRDG
RDCEAADRQP YHRSRSTEQR PLLERTTTRS RSTERPDTNL MRSMPSLMTG RSAPPSPALS
RSHPRTGSVQ TSPSSTPVAG RRGRQLPQLP PKGTLERNNG VKEIEPYEEE VDSTRRRHAG
AMDIEERNRQ MKINKYKQVA GSDPRLEQDY HSKYRSGWDP HRGADNISTK SSDSDVSDIS
AVSRTSSASR FSSTSYMSVQ SERPRGNKKI SVFTSKMQSR QMGVSGKNMA KSTSISGDMC
SLEKTDGSQS DTAVGALGTS GKKRRSSIGA KMVAIVGLSR KSRSASQLSQ TEAGGKKLRS
TVQRSTETGL AVEMRNWMTR QASRESTDGS MNSYSSEGNL IFPGVRLASD SQFSDFLDGL
GPAQLVGRQT LATPAMGDIQ VGMMDKKGQL EVEIIRARGL VVKPGSKTLP APYVKVYLLD
NGVCIAKKKT KVARKTLEPL YQQLLSFEES PQGKVLQIIV WGDYGRMDHK SFMGVAQILL
DELELSNMVI GWFKLFPPSS LVDPTLAPLT RRASQSSLES STGPSYSRS
//
