ID A0A3Q1FX22_9TELE Unreviewed; 1447 AA.
AC A0A3Q1FX22;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 1-like {ECO:0000313|Ensembl:ENSAPOP00000021029.1};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSAPOP00000021029.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000021029.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000021029.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSAPOT00000017320.1; ENSAPOP00000021029.1; ENSAPOG00000001369.1.
DR GeneTree; ENSGT00940000155134; -.
DR Proteomes; UP000257200; 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: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; 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:UP000257200};
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 23..163
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 84..151
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 555..647
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 699..822
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1293..1411
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 158..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..75
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 158..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 159981 MW; 953AF289C27A4921 CRC64;
MSASVGPQGG PRPPTVPPSM PDLPDLSHLT EEERKIIMAV MARQKEEEEK EQAMLKTLHQ
QFESYKQEVR RIGAETRRQQ TLQKDDAPTC GICRKTKFAD GCGHLCSYCQ TKFCARCGGR
VSLRSNNEDK VCLIVKDRVM WVCNLCRKQQ EILTKSGEWF SGSGVRPGSQ GNSLTDPATG
GEAQRDTKLL RSRSQAPPSS TNSGPQTGVP AVKRTDTMLG SRSQSEPPRE KKRPVSLHEQ
NGKGGMGRGS GRRPAGKVQS QSSLDERIGP AERERRLGDG RRLEKIHSQD YEDGDENLSR
SEKHRRRPED EEQRERQRRE EEFQNRYRSD PNLARYPVKP QKEEQEMRMH AKVSKVRHER
RHSDLAINEV GLEGGSGGGG AGEVPENRLA RRGGSGEGDR KVPLENHRAY SVDRTVGGGA
PPAGGGGRSG PQTGGPASLD WGPSNGRLEP TRTSRDKGGD NLLRKDSQSS DQSESLRPPP
PRSHKSKRGV NRRQMSISSS EEEGGSTPEY TSCEDVDMES VSEKGDWDCH SLDPAVCHHP
VTWQPSKEGD HLIGRITLSK RSAMPREAGS LLGLKVVGGK MTETGRLGAF ITKVKKGSLA
DVVGHLRAGD EVLQWNGKSL PGATKKEVYN IILESKAEPL VEIVVSRPIG DIPRIPASPH
PPLESTGSSS FESQKMDRPS ISVMSPTSPG TLRDLPLVLP GQLSVKLWYD KVGHQLIVNV
LQAIDLPARP DGRPRNPYVK MYFLPDRSDK SKRRTKTVKK SAEPKWNQTF LYSHVHRRDF
RERMLEITVW DQPRVQEEES EFLGEILIVL ETALLDDIPH WYKLQTHDVS SIPLPQPSPY
LPRRHGGHGD SPSKKLQRSH RIIDTEFDDG LVVVTKGAER NSRERERGSM LAVPEQQRPV
QHRSRSVSPH REDSCRARSR PAHVPMQRSL DEIHQNRHHS PSLYHEPHLE HQRSGDSDYE
YSEDSEVLEM HRSVRGGSAE CLHTNSDLQP SLDRVRSAST TCLRPDSNFH SPDRDRAHPH
GSPSPPTGTP SSGRRGRQLP QLPAKSSSIE QVLTVEDRAR QLPMKVHSYR PSASHDPKLD
LKTKREMYAE RRRSSDNMSA RSSDSELSDG SALSRASSAS HLSYISVQSE RPGGRLSRQV
RSMGGSMLKS SSVSGEIYTQ ERTDGSQSDT ALGTVGGGSK KRRSSLSARV VAIVGNRRSR
STSQISGPEG KSKKEKGAPI KRSTETGMAV ELPRNMSRQP SRESNNGSMN SYNSEGNLIF
SGVNLGASSQ FSDFLDGLGP AQLVGRQTLA TPAIGDIQIA MMEKKGQLEV EVIRARGLVQ
KPGSKSLPAP YVKVYLLNNG AYVAKKKTKI ARKTLDPLYQ QALLFEESPQ GKVLQVIVWG
DYGRMDHKSF MGVAQILLEE LDLSSTAIGW YKLFPPSSLV DPTLASLTRR ASQSSLDSSS
GPPGVRS
//
