ID A0A087YGQ1_POEFO Unreviewed; 1326 AA.
AC A0A087YGQ1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=RIMS binding protein 2 {ECO:0000313|Ensembl:ENSPFOP00000017204.2};
GN Name=RIMBP2 {ECO:0000313|Ensembl:ENSPFOP00000017204.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000017204.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000017204.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RIMBP family.
CC {ECO:0000256|ARBA:ARBA00010749}.
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DR EMBL; AYCK01011777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000017226.2; ENSPFOP00000017204.2; ENSPFOG00000017077.2.
DR GeneTree; ENSGT00950000183203; -.
DR OMA; KEEAYCR; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR CDD; cd00063; FN3; 2.
DR CDD; cd12014; SH3_RIM-BP_1; 1.
DR CDD; cd12012; SH3_RIM-BP_2; 1.
DR CDD; cd12013; SH3_RIM-BP_3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035753; RIM-BP_SH3_2.
DR InterPro; IPR035755; RIM-BP_SH3_3.
DR InterPro; IPR040325; RIMBP1/2/3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14234; RIM BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR14234:SF18; RIMS-BINDING PROTEIN 2; 1.
DR Pfam; PF07653; SH3_2; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 186..253
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 499..598
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1122..1190
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1226..1293
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 254..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 644..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1326 AA; 148844 MW; F9C4745AE29EBA79 CRC64;
MREAAERRQQ LELEHEQALA VLNAKQQEID LLQKAQVEAK KEHEGAVHLL EAKVRELEEK
CRSQSEQFNL LSKELEKFRL QAGKFDILST EPLTLSESPG SPNKSLSQLL NGLAAPIEKG
SEGPTSRSLI SEFIRPLQIS GDKPELLSVK PTFLSRSRAS SPARAFLSEM DKELSSTTRS
KPRFTGKVRL CVARYSYNPY DGPNEHPEAE LPLVAGKYLY VYGTMDEDGF YSGELLDGQR
GLVPSNFVEF VQDDDTPSAQ HRNTTVKEPG YLNHSSLGPP RHSSGTGTSN GTGTLDVSID
EVGEDIVPYP RRINLIKQLA KSVIIGWDPP VLPPGWGSIS GYNVLVDKEV RMSVPYGGRT
KSLIEKLNLA TNTYRISVQS ITDRGPSDEL RCSLLVGKDV VVAPYYLRVD GITQSSAELS
WMPSNSNYSH TIFLNGAEYD MVKAGGYRYK FFNLKSMTVY KVKVVAQPHQ VPWQLPGDQR
EKREISVEFC TQPAGPPLPP QEVQVQCGQT PGVLQVRWKP PPLTPSGTSN GASVIGYAVC
TKGQKIAEVL YPTADFVSVD LNRIQGLEAR EVIVRTLSTQ GESQDSPVAM IPPHSQPVCH
PPPPHPQLHF QRHSIPKSKP LISAREPETK EHEVGLRLAQ PWERAPSPLP PMHGANLEPP
HFPPRRSPSP QRILPQPQGV PIPNTIAKAM AREAAQRAFA EGNRVEKRNI FSDRGNALHP
LNSDEEEDGY DSPHARRRGA SVDEFLRGSE LGRQHHHHHY SHSEEYHTES SRGSDLSDIM
EEDEEDLYSE MQLEEGRRRS INSHSTLKRQ DLAEERDCWD LQREVVKQRS LRSKRLHSIP
EVAEEESDSL DSMGQHLSFE EGGRPGTPHT QRRMYPQESH HARDHLTPGK NSRLQRQRSS
PRFSDSRYGY GADDRSYGRP SRQNTKSPDS GLDCGSEEEG SLGRGHRGYY AHGSPIRGPV
RIIHCEGPVE RRALAMGRKR TLTRQCSVEE EFSDAEGALS EGRLNELDRV YYSPHREART
QSLSRLNRDQ PLVCESEFLL YFLSASCKLT KTQHRNRIAP KIIGNSPSHG SPDRLDHSGR
RPVHIGTPPQ RRPIPSIDGY GGRRHGRGRQ SPDYFEESES EDLTRVFVAL FDYDPLSMSP
NPDAADEELP FKEGQIIKVF GNKDTDGFYR AEIRGRVGLI PCNMVSEIQT EDDEMMDQLL
KQGFLPLNTP VEKLERNRRS GRQYPTSTWR MVALYDYDPR ESSPNVDVEA ELTFCAGDVI
TVFGEIDEDG FYYGELNGHK GLVPSNFLEE VPDDVDVFLT DSPSRYPQDT PFTCLAKQKK
SVHFTP
//
