ID A0A3Q1MH95_BOVIN Unreviewed; 1604 AA.
AC A0A3Q1MH95;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Regulating synaptic membrane exocytosis 1 {ECO:0000313|Ensembl:ENSBTAP00000068442.1};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSBTAP00000068442.1,
GN ECO:0000313|VGNC:VGNC:53801};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000068442.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000068442.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000068442.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000068442.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000068442.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSBTAT00000066372.1; ENSBTAP00000068442.1; ENSBTAG00000020238.7.
DR VEuPathDB; HostDB:ENSBTAG00000020238; -.
DR VGNC; VGNC:53801; RIMS1.
DR GeneTree; ENSGT00940000155134; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000020238; Expressed in prefrontal cortex and 53 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MH95; baseline.
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:UP000009136};
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..191
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 119..179
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 608..694
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 745..868
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1450..1568
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1604 AA; 177876 MW; 7BE45B826DB98DBE CRC64;
MSSAVGPRGP RPPTVPPPMP ELPDLSHLTE EERNIILAVM DRQKEEEEKE EAMLKCVVRD
MVKPAACKAP RNVEHQPHQP PPLCPFSLLS RRLHQQFESY KEQVRKIGEE ARRYQGEHKD
DAPTCGICHK TKFADGCGHL CSYCRTKFCA RCGGRVSLRS SNVSTVVMWV CNLCRKQQEI
LTKSGAWFFG SGPQQPSQDG TLSDTATGAG SEAPREKKAR LQERSRSQTP LSSAAASAQD
QATPGAQVDR TKGAEPAPQA GGPEQKQASS RSRSEPPRDR KKTPGLAEQN GKGAPKGERK
RAPRTSAPPA EAPAEERERK ERRESRRLEK GRSQDYSVVP EKREEGPVAE AEKQRKEEEY
QTRYRSDPNL ARYPVQPPPE EQQMRMHARV SRARHERRHS DVSLPRTEAA AGPEGRPGPR
APHAARGSPP ASPRAYSAER TAEARAPGAQ PLADSSPPAP RPGPGPAEVP EPLRKQSRLD
PGSAVLVRKA KREKVETMLR NDSLSSDQSE SVRPSPPKPH RAKRGGKRRQ MSVSSSEEEG
VSTPEYTSCE DVELESESVS EKGDLDYYWL DPATWHSRET SPISSHPVTW QPSKEGDRLI
GRVILNKRTT MPKESGALLG LKVVGGKMTD LGRLGAFITK VKKGSLADVV GHLRAGDEVL
EWNGKPLPGA TNEEVYNIIL ESKSEPQVEI IVSRPIGDIP RIPESSHPPL ESSSSSFESQ
KMERPSISVI SPTSPGALKD APQVLPGQLS VKLWYDKVGH QLIVNVLQAT DLPPRVDGRP
RNPYVKMYFL PDRSDKSKRR TKTVKKVLEP KWNQTFVYSH VHRRDFRERM LEITVWDQPR
VQEEESEFLG EILIELETAL LDDEPHWYKL QTHDESSLPL PQPSPFMPRR HTHGESASKK
LQRSQRISDS DMSDYEVDDA IGVVPPVGYR SSTRESKPST LTVPEQQRTT HHRSRSVSPH
RGDDQGRPRS RLPNVPLQRS LDEIHPTRRS RSPTRHRDAS RSPIDQRIRD VDSQCLSEQD
SELLMLPRAK RGRSAECLHT TSDLQPSLDR ARSASTNCLR PDASLHSPER ERHSRKSERS
SIQSQTRKGT ASDAERVLPP CLSRRGYAAA RATDQPVLRG KHPARSRSSE HPSVRTLCSM
HHLAPGGSAP PSPLLTRSTH RQASPTRSPP MDAAFSSRRG RQLPQVPVRS GSIEQASLVV
EERTRQMKMK VHRFKQTTGS GSSQELDREQ YSKYNAHTDQ YRSCDNVSTR SSDSDVSDAS
AVSRTSSASR LSSTSFLSEQ SERPRGRISS FTPKMQGRRM GTSGRAITKS TSMSGEMYTL
EHNDGSQSDT AVGTVGAGGK KRRSSLSAKV VAIVSRRSRS TSQLSQTESG HKKLKSTIQR
STETGMAAEM RKMVRQPSRE STDGSINSYS SEGNLIFPGV RLGADSQFSD FLDGLGPAQL
VGRQTLATPA MGDIQIGMED KKGQLEVEVI RARSLTQKPG SKSTPAPYVK VYLLENGACI
AKKKTRIARK TLDPLYQQSL VFDESPQGKV LQVIVWGDYG RMDHKCFMGV AQILLEELDL
SSMVIGWYKL FPPSSLVDPT LTPLTRRASQ SSLESSTGPP CIRS
//
