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Database: UniProt
Entry: A0A3P8PW09_ASTCA
LinkDB: A0A3P8PW09_ASTCA
Original site: A0A3P8PW09_ASTCA 
ID   A0A3P8PW09_ASTCA        Unreviewed;      1419 AA.
AC   A0A3P8PW09;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Regulating synaptic membrane exocytosis 1a {ECO:0000313|Ensembl:ENSACLP00000021193.1};
GN   Name=RIMS1 {ECO:0000313|Ensembl:ENSACLP00000021193.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000021193.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000021193.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000021193.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSACLT00000021683.1; ENSACLP00000021193.1; ENSACLG00000014225.1.
DR   GeneTree; ENSGT00940000155134; -.
DR   Proteomes; UP000265100; Chromosome 13.
DR   Bgee; ENSACLG00000014225; Expressed in brain 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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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   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          21..178
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          106..166
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          506..599
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          651..776
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1265..1383
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          171..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1160..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..820
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..891
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1160..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1419 AA;  155201 MW;  DB52A8A0774C8E0C CRC64;
     MFASVGPRGG PRPPVAPAIP EPDLSHLTED ERKIIMAVLA RQREEEAKEE AMLKEEKPIQ
     ARTVNLVGQK KPPQQNDVRG IQQQLSSYRE TVIRQATAAA GSAIHRDDAP TCGICHKTKF
     ADGCGNPCSY CQTKFCARCG GRVSLRSNTE DKVVIWVCNN CRKQQEILTK PGEWFTGPPG
     KPAGLGSAVS EPSVCQAPGD KKLRSRSQAP PGSTTAIYDP NRPSAPGTAP GTDARSLSEP
     PRDTRNGRGG GAGRGERRQG QPRLKTQVSM DRDLRGESRE RRESRRLTKG RSLEHDPVGG
     VGVRRTEEGD YHHMDHTGAP PRQAGPVPPG GRGHPVPGQG RGTGVGGGEV GDGARPGQRT
     AGGVGGLHEH ALSQQAPPPE LREPPDSGPG SAPGQGPSVK RTKRDKAESM LRNDSLSSDQ
     SESLRPPPPR PYKSKRGQGA GGKRQTSVSS SEEEGGTTPE YSSCEDAEIE SVSERGDWEC
     YPHDPTVWHH PVTWQPSKEG DHLIGRITLS KRTAAMPKEA GALLGLKVVG GRVTESGRLG
     AFITKVKKGS LADVVGHLRA GDEVLQWNGK LLPGATMKEV YNIILESQAD PQVELVVSRP
     IGDIPRIPDT SHPPLESTGS SSFESQKMER PSLNVLSPSS PGMLRDAPQL MPGRLSVKLW
     YDKVGHQLIV NVLQAVELSL RPDGRPRSPY VKMYFLPDRS DKSKRRTKTV KKTCEPKWNQ
     TFVYSHVHRR DFRNHMLELT VWDQPRSPEE DSIFLGEVLV ELETALLDDK PHWYPLQTHD
     VSSIPLPQPS PYLPRRHIDA PGKKLQPDGR GRERQREPTS TLEVPEQQRT PTHHIRSRSV
     SPHREEQGRI RSRPPNVPPQ RSLDDELSHG HRSRSPSRYY DAGRGRHQGE GYLDDSEVFT
     IHQSMRGKSA ECLHTRRPTR HNNTLPPKMP LLFSSFRKQA NSDLQPSLDR VRSASANCLA
     PNNHAPSPET ERGHLQSGGS LSSSVTSSST RRVRQLPQLP PKSSTVEQAL VAEERVRQLQ
     MRVHSNRVSA PATSSQQDLD RALKNKRELY KDQRRSSENV SHKSSDSDVS DVSAISRTSS
     ASRISSTSYM SIQSERPRGR FSRAMRASGR HMMKSTSISG EIYGMEHADG SQSDTALGSL
     GSGIKKRRSS LSQRVVAILP SRRSRSTSQL SQTEASAGKK VGKAGSSSIQ RSVETGMAVE
     YPRGGSAMNR QASRESTDGS MNSYSSEGNL IFSGMRLGAD SQFSDFLDGL GPGQLVGRQT
     LATPAMGDVQ IGLMDKKGQL EVEVIRARGL TPKPGSKSLP APYVKVYLLD NGTCKAKKKT
     KIARKTLEPL YQQHLLFDES PQGKVLQVIV WGDYGRLDHK CFMGVAQILL EELDLSSTVI
     GWYKLFPPSS LVDPTLAPLT RLASQTSLDS SGPPPGVRS
//
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