ID A0A2R8M4B8_CALJA Unreviewed; 1540 AA.
AC A0A2R8M4B8;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Regulating synaptic membrane exocytosis 1 {ECO:0000313|Ensembl:ENSCJAP00000053520.3};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSCJAP00000053520.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000053520.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000053520.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000053520.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSCJAT00000067610.3; ENSCJAP00000053520.3; ENSCJAG00000009737.5.
DR GeneTree; ENSGT00940000155134; -.
DR Proteomes; UP000008225; Chromosome 4.
DR Bgee; ENSCJAG00000009737; Expressed in cerebellum and 2 other cell types or tissues.
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:UP000008225};
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 24..184
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 112..172
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 607..693
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 744..867
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1387..1505
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 172021 MW; 9C80E6DD2E837D74 CRC64;
MKMSSAVGPR GPRPPTVPPP MQELPDLSHL TEEERNIIMA VMDRQKEEEE KEEAMLKCVV
RDMAKPAACK TPRNAENQPH QPTPRLHQQF ESYKEQVRKI GEEARRYQGE HKDDAPTCGI
CHKTKFADGC GHLCSYCRTK FCARCGGRVS LRSSNEDKVV MWVCNLCRKQ QEILTKSGAW
FFGSGPQQTS QDGTLSDTTT GTGSEVPREK KARLQERSRS QTPLSTAAAS SQDSAPPSAP
PDSSKGVEPS QQALGPEQKQ ASSRSRSEPP RERKKTPGLS EQNGKGAPRS ERKRVPKTSA
QPGEAAVEER ERKERRESRR LEKGRSQDYA DVPEKRDDGK AADEEKQRKE EEYQTRYRSD
PNLARYPVKP PPEEQQMRMH ARVSRARHER RHSDVALPRT EEGAALPEGK VGKRAPVAAR
ASPPDSPRAY SAERTAETRT PGAKQLTNHS PPAPRHGPVS AEAPELKAQE PLRKQSRLDP
SSAVLIRKAK 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 LPARVDGRPR
NPYVKMYFLP DRSDKSKRRT KTVKKILEPK WNQTFVYSHV HRRDFRERML EITVWDQPRV
QEEESEFLGE ILIELETALL DDEPHWYKLQ THDESSLPLP QPSPFMPRRH IHGESSSKKL
QRSQRISDSD ISDFEVDDGI GVVPPVGYRS SVREGKSTTL TVPEQQRTTH HRSRSVSPHR
GNDQGRPRSR LPNVPLQRSL DEIHPIRRSR SPTRHHDASR SPVDHRARDV DSQYLSEQDS
ELLMLPRAKR GRSAECLHTT SELQPFLDRA RSASTNCLRP DTSLHSPERE RHSRKSERSS
IQKQTRKGTA SDAERMHRQR SPTQSPPADT SFSSRRGRQL PQVPVRSGSL EQASLVVEER
TRQMKMKVHR FKQTTGSGSS QELDREQYSK YNIHKDQYRS CDNVSAKSSD SDVSDVSAIS
RTSSASRLSS TSFMSEQSER PRGRISSFTP KMQGRRMGTS GRAIMKSTSV SGEMYTLEHN
DGSQSDTAVG TVGAGGKKRR SSLSAKVVAI VSRRSRSTSQ LSQTESGHKK LKSTIQRSTE
TGMAAEMRKM VRQPSRESTD GSINSYSSEG NLIFPGVRLG ADSQFSDFLD GLGPAQLVGR
QTLATPAMGD IQIGMEDKKG QLEVEVIRAR SLTQKPGSKS TPAPYVKVYL LENGACIAKK
KTRIARKTLD PLYQQSLVFD ESPQGKVLQV IVWGDYGRMD HKCFMGVAQI LLEELDLSSM
VIGWYKLFPP SSLVDPTLTP LTRRASQSSL ESSTGPPCIR
//
