ID A0A452E725_CAPHI Unreviewed; 1537 AA.
AC A0A452E725;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Regulating synaptic membrane exocytosis 1 {ECO:0000313|Ensembl:ENSCHIP00000007849.1};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSCHIP00000007849.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000007849.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000007849.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000007849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000015600.1; ENSCHIP00000007849.1; ENSCHIG00000011011.1.
DR GeneTree; ENSGT00940000155134; -.
DR Proteomes; UP000291000; Chromosome 14.
DR Bgee; ENSCHIG00000011011; Expressed in cerebellum and 12 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 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; 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; 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; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
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 67..123
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 543..629
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 680..803
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1383..1501
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 135..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1537 AA; 170367 MW; B3F208E6EE9A5A59 CRC64;
LNLIQFPGSP RPPTVIIEEK VFFFSAPSST LCPFSLLSRR LHQQFESYKE QVRKIGEEAR
RYQGEHKDDA PTCGICHKTK FADGCGHLCS YCRTKFCARC GGRVSLRSNN VMWVCNLCRK
QQEILTKSGA WFFGSGPQQP SQDGTLSDTA TGAGSEAPRE KKARLQERSR SQTPLSSAAA
SAQDQAAPGA QMDRTKGAEP APQAGGPEQK QASSRSRSEP PRDRKKTPGL AEQNGKGAPK
GERKRAPRTS APPAEAPAEE RERKERRESR RLEKGRSQDY SVVPEKREEG PVAEAEKQRK
EEEYQTRYRS DPNLARYPVQ PPPEEQQMRM HARVSRARHE RRHSDVSLAR TEAAAGPEGR
PGPRAPHAAR GSPPASPRAR APGAQPLADP SPPAPRPGPG PAEVPEPLRK QSRLDPGSAV
LVRKAKREKV ETMLRNDSLS SDQSESVRPS PPKPHRAKRG GKRRQMSVSS SEEEGVSTPE
YTSCEDVELE SESVSEKGDL DYYWLDPATW HSRETSPISS HPVTWQPSKE GDRLIGRVIL
NKRTTMPKES GALLGLKVVG GKMTDLGRLG AFITKVKKGS LADVVGHLRA GDEVLEWNGK
PLPGATNEEV YNIILESKSE PQVEIIVSRP IGDIPRIPES SHPPLESSSS SFESQKMERP
SISVISPTSP GALKDAPQVL PGQLSVKLWY DKVGHQLIVN VLQATDLPPR VDGRPRNPYV
KMYFLPDRSD KSKRRTKTVK KVLEPKWNQT FVYSHVHRRD FRERMLEITV WDQPRVQEEE
SEFLGEILIE LETALLDDEP HWYKLQTHDE SSLPLPQPSP FMPRRHPHGE SASKKLQRSQ
RISDSDMSDY EVDDAIGVVP PVGYRSSTRE SKPSTLTVPE QQRTTHHRSR SVSPHRGDDQ
GRPRSRLPNV PLQRSLDEIH PTRRSRSPTR HRDASRSPID QRIREVDSQC LSEQDSELLM
LPRAKRGRSA ECLHTTSDLQ PSLDRARSAS TNCLRPDASL HSPERERHSR KSERSSLQSQ
TRKGTASDAE RVLPPCLSRR GYAAARATDQ PVLRGKHPAR SRSSEHPSVR TLSMHHLAPG
GSAPPSPLLT RTHRQASPSR SPPTDAAFSS RRGRQLPQVP VRSGSIEQAS LVVEERTRQM
KMKVHRFKQT TGSGSSQELD REQYSKYSAH TDQYRSCDNV SARSSDSDVS DASAVSRTSS
ASRLSSTSFL SEQSERPRGR ISSFTPKMQG RRMGTSGRAI TKSTSMSGEM YTLEHNDGSQ
SDTAVGTVGA GGKKRRSSLS AKVVAIVSRR SRSTSQLSQT ESGHKKLKST IQRSTETGMA
AEMRKMVRQP SRESTDGSIN SYSSEGNLIF PGVRLGADSQ FSDFLDGLGP AQLVGRQTLA
TPAMGDIQIG MEDKKGQLEV EVIRARSLTQ KPGSKSTPAP YVKVYLLENG ACIAKKKTRI
ARKTLDPLYQ QSLVFDESPQ GKVLQVIVWG DYGRMDHKCF MGVAQILLEE LDLSSMVIGW
YKLFPPSSLV DPTLTPLTRR ASQSSLESST GPPCIRS
//
