ID A0A287A8N9_PIG Unreviewed; 1474 AA.
AC A0A287A8N9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Regulating synaptic membrane exocytosis 1 {ECO:0000313|Ensembl:ENSSSCP00000040157.2};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSSSCP00000040157.2,
GN ECO:0000313|VGNC:VGNC:92309};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000040157.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000040157.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000040157.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000040157.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSSSCT00000054435.2; ENSSSCP00000040157.2; ENSSSCG00000004280.5.
DR VGNC; VGNC:92309; RIMS1.
DR GeneTree; ENSGT00940000155134; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000004280; Expressed in cerebellum and 32 other cell types or tissues.
DR ExpressionAtlas; A0A287A8N9; 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 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287A8N9};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 604..690
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 741..864
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1320..1438
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1277
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 182..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..243
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..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 164025 MW; C4DE8262D3873B5E CRC64;
MSSAVGPRGP RPPTVPPPMP ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MVKPAACKTP RNAEHQPHQP PPRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICR
KTKFADGCGH LCSYCRTRFC ARCGGRVSLR SNSEDKVVMW VCNLCRKQQE ILTKSGAWFF
GSGPQQPSQD GTLSDTATGA GSEAPREKKA RLQERSRSQT PLSTAAASSQ DQAPSSAQPD
RSKGAELSQP AGGPEQKQAS SRSRSEPPRD RKKTPGLSEQ NGKGAPKGER KRVPRSSVQP
GEGPAEERER KERRESRRLE KGRSQDYPDV PEKREDGPAV EDEKQRKEEE YQTRYRSDPN
LARYPVKPPP EEQQMRMHAR VSRARHERRH SDVALPRTEA AAGPEGRAGP RAPAAARGSP
PASPRAYSAE RTADARAPSA QQLANRSPPA PRPGPGPADV PESRAPEPLR KQSRLDPGSA
VLVRKAKREK VETMLRNDSL SSDQSESVRP SPPKPHRAKR GGKRRQMSVS SSEEEGVSTP
EYTSCEDVEL ESESVSEKGD LDYYWLDPAT WHSRETSPIS SHPVTWQPSK EGDRLIGRVI
LNKRTTMPKE SGALLGLKVV GGKMTDLGRL GAFITKVKKG SLADVVGHLR AGDEVLEWNG
KPLPGATNEE VYNIILESKS EPQVEIIVSR PIGDIPRIPE SSHPPLESSS SSFESQKMER
PSISVISPTS PGALKDAPQV LPGQLSVKLW YDKVGHQLIV NVLQATDLPP RVDGRPRNPY
VKMYFLPDRS DKSKRRTKTV KKVLEPKWNQ TFVYSHVHRR DFRERMLEIT VWDQPRVQEE
ESEFLGEILI ELETALLDDE PHWYKLQTHD ESSLPLPQPS PFMPRRHIHG ETSSKKLQRS
QRISDSDISD YEVDDGIGVV PPGYRSSARE GKPTTLTVPE QQRTTHHRSR SVSPHRGDDQ
GRPRSRLPNV PLQRSLDEIH PTRRSRSPTR HHDASRSPVD HRSRDVDSQY LSEQDSELLM
LPRAKRGRSA ECLHTTRMHR QGSPTQSPPA DSAFSSRRGR QLPQVPVRSS SIEQASLVVE
ERTRQMKMKV HRLKQTAGSG SSQELDREQY SKYNIHKDQY RSCDNVSAKS SDSDVSDVSA
ISRTSSASRL SSTSFLSEQS ERPRGRIRRM GTSGRAIIKS TSVSGEMYTL 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
//
