ID W5NH40_LEPOC Unreviewed; 1698 AA.
AC W5NH40;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Regulating synaptic membrane exocytosis 1a {ECO:0000313|Ensembl:ENSLOCP00000019949.1};
GN Name=RIMS1 {ECO:0000313|Ensembl:ENSLOCP00000019949.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019949.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019949.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01001663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000019949; -.
DR Ensembl; ENSLOCT00000019982.1; ENSLOCP00000019949.1; ENSLOCG00000016181.1.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00940000155134; -.
DR HOGENOM; CLU_001061_1_0_1; -.
DR InParanoid; W5NH40; -.
DR OMA; QASNTIC; -.
DR Proteomes; UP000018468; Linkage group LG16.
DR Bgee; ENSLOCG00000016181; Expressed in camera-type eye and 6 other cell types or tissues.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
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..179
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 107..167
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 590..676
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 727..850
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1544..1662
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 37..105
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 209..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1698 AA; 190811 MW; C727D1C5085551C9 CRC64;
MSASLGSHGP RPPTAPPSMQ DLPDLSHLTE EERKIIMAVM VRQKEEEEKE EAMLKDENPI
EARTVLVLGK KLPEQIEIRR LHQQFESYKE QVRKIGEEAR RYQGEHKDDA PTCGICRKTK
FADGCGHICS YCQTKFCARC GGRVSLRSNN EDKVVMWVCN LCRKQQEILT KSGEWFFGRG
SQASSLDGAL SDTAMRGDVP REKKVRSRSQ IPLSTAAGSQ EAPQPVLATE RSKGADSALQ
AMPSSRSRSE PPRDRKKPSA IPEQNGKAGV KNERKRVPKS AAQHGERQIE DKEHKERRES
RRLEKGRSQD YPDMDEGRKK AEEEKQRKEE EFQTRYRSDP NLARYPIKPQ PEEQEMLIHA
KVSKARHQRR HSDVALANTE AEGSEVLENR LGRRSQPPGA EEHKSPMENH RSYSIERTGN
VQISVSKQMA NHSPPTARHS LVPASQLESK DQDWGKKQCH LDPSSAAIIR KTKREKMETM
LRNDSLSSDQ SESLRPPPPK PYKTKRGGNK RQMSVSSSEE EGGSTPEYTS CEDVEIESES
VSEKGDWDCF PLDPAIWHVS ETSPISSHPV TWQPSKEGDH LIGRIILSKR TTMPKESGSL
LGLKVVGGKI TETGRLGAFI TKVKKGSLAD AVGHLKAGDE VLQWNGKSLP GATKKEVYNI
ILESKSELQV EIVVSRPIGD IPRIPETSHP PLESSSSSFE SQKMERPSIS VISPTSPGTL
RDAPQVLPGQ LSVKLWYDKV GHQLIVNVLQ ATGLPARSDG RPRNPYVKMY FLPDRGDKSK
RRTKTVKKSL EPKWNQTFLY SHVHRRDFRE RMLEITVWDQ PRVQEEASEF LGEILIELET
ALLDDEPHWY KLQTHDVSSL PLPQPSPYMP RRHIHGESPC KKLQTAECRS SSKERKSTTL
TVPEQQRVAH HRSRSVSPHR GDDQGRTRSR PPSVPLQRSL DEIHQSRQSR SPTRYHDASR
SKDDRRSRDG DSQYFPEESE FLMLPRAKRG RSAECLHTKR SSIKYSKTLP PKMPLLVNGI
HRNIYSSTLP ACLKTKSLLR KDPPNPRTSF NTRVLRFTDE IMSSDLQPSL DRLRSASTNC
LRPDTSFHSP ERERSSQSLP RRRPTSPRIL IQHASPEDDR QSRTLERSSS QKHSRKNSAP
ESERERLTSS GRGISSAPRS PDHLSVKERK PTRSRSSERP SERMFRSVYQ ITPGGSAPAS
PLMHRAHQHG SLSQSPPSGT PLSGRRGRQL PQVPVKSSSI EQALAVEERA RQLQMKVHSY
KTSAMSSSSQ ELERELKTKR ELYKEQHRSC DNVSTRSSDS DISDVSAISR TSSASRLSST
SYMSIQSERP RGRIRSKSLE SCKGEEKKER RISWELNGRE EKHEHTERKH STEDLSRRRH
SVAGDMSRQM RPSGRSMMKS TSVSGEIYNL ERNDGSQSDT AIGTVGTGGK QRRSSLSARV
VAIVGLPSRR SRSTSQLSQT AANKKLKSQI QRSQETGMAV EYPRNAMARQ ASRESTDGSM
NSYSSEGNLI FSGMRLGADS QFSDFLDGLG PAQLVGRQTL ATPAMGDIQI GMMDKKGQLE
VEVIRARGLT PKPGSKSLPA PYVKVYLLEN GACIAKKKTK IARKTLDPLY QQSLLFEESP
QGKVLQVIVW GDYGRMDHKC FMGVAQILLE ELELSSTVIG WYKLFPPSSL VDPTLAPLTR
RASQSSLESS TGPPCIRS
//
