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RIMB2_CHICK
ID   RIMB2_CHICK             Reviewed;        1325 AA.
AC   Q8QFX1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=RIMS-binding protein 2;
DE            Short=RIM-BP2;
GN   Name=RIMBP2; Synonyms=RBP2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INTERACTION WITH RIMS1; RIMS2; CACNA1D AND CACNA1B, AND
RP   FUNCTION OF SH3 DOMAIN.
RX   PubMed=11988172; DOI=10.1016/s0896-6273(02)00667-0;
RA   Hibino H., Pironkova R., Onwumere O., Vologodskaia M., Hudspeth A.J.,
RA   Lesage F.;
RT   "RIM binding proteins (RBPs) couple Rab3-interacting molecules (RIMs) to
RT   voltage-gated Ca(2+) channels.";
RL   Neuron 34:411-423(2002).
CC   -!- FUNCTION: Plays a role in the synaptic transmission as bifunctional
CC       linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and
CC       CACNA1B. {ECO:0000269|PubMed:11988172}.
CC   -!- SUBUNIT: Interacts with RIMS1, RIMS2, CACNA1D and CACNA1B, and
CC       potentially with other Ca(2+) channel alpha-1 isoforms.
CC       {ECO:0000269|PubMed:11988172}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11988172}.
CC       Synapse {ECO:0000269|PubMed:11988172}. Note=Synaptic plasma membrane.
CC   -!- TISSUE SPECIFICITY: Brain, cochlea and retina.
CC       {ECO:0000269|PubMed:11988172}.
CC   -!- DOMAIN: The SH3 domains mediate binding to a proline-rich motif in
CC       RIMS1, RIMS2, CACNA1D and CACNA1B.
CC   -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
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DR   EMBL; AY072908; AAL67995.1; -; mRNA.
DR   RefSeq; NP_989586.1; NM_204255.1.
DR   AlphaFoldDB; Q8QFX1; -.
DR   SMR; Q8QFX1; -.
DR   STRING; 9031.ENSGALP00000004056; -.
DR   PaxDb; Q8QFX1; -.
DR   GeneID; 374105; -.
DR   KEGG; gga:374105; -.
DR   CTD; 23504; -.
DR   VEuPathDB; HostDB:geneid_374105; -.
DR   eggNOG; KOG3632; Eukaryota.
DR   InParanoid; Q8QFX1; -.
DR   OrthoDB; 102427at2759; -.
DR   PhylomeDB; Q8QFX1; -.
DR   PRO; PR:Q8QFX1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd12012; SH3_RIM-BP_2; 1.
DR   CDD; cd12013; SH3_RIM-BP_3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035519; RIM-BP2.
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; PTHR14234; 1.
DR   PANTHER; PTHR14234:SF18; PTHR14234:SF18; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF50044; SSF50044; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Repeat; SH3 domain; Synapse.
FT   CHAIN           1..1325
FT                   /note="RIMS-binding protein 2"
FT                   /id="PRO_0000221386"
FT   DOMAIN          186..253
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          315..408
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          411..493
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          507..608
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1121..1189
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1225..1292
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          153..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1325 AA;  147538 MW;  1DD8C50D4CDA1B5B CRC64;
     MREAAERRQQ LELEHEQALA VLNAKQQEIE LLQKAQVEAK KEHEGAVQLL EAKVRELEEK
     CRTQSEQFNL LSRELEKFRQ QAGKIDLLSS NPLTSSDISG SPSKSLSQLM NGIATSLGKG
     HESPSGSRCV ISEFIRPLQI SGDKPEQLSV KPTFLSKSRS DTPRCRFDSD MDNDQNSNTS
     KQRYSGKVHL CIARYSYNPF DGPNENPEAE LPLTAGKYLY VYGDMDEDGF YEGELLDGQR
     GLVPSNFVDF VQDNETRLSS TLSSEQDQNF INHSGSTLEG DILEISPPSH IDSSVISNGA
     GTLDVNIDEI GEDIVPYPRK ITLIKQLAKS VIVGWEPPVV PPGWGTINSY NVLVDKEVRM
     NIALGSRTKA LIEKLNISTC TYRISIQSIT NKGNSDELQC TLLVGKDVVV APSNLKVDNI
     TQISAELSWL PTNSNYSHVI FLNEEEFDIV KAASYKYHFF NLKPNMAYKV KVMAKPHQMP
     WQLPLEQREK KEAFVEFSTL PAGPPAPPQD VTVRAGSTQA TIQVSWKPPA LTATGTSHGA
     NVTGYGVYAK GQRVAEVIFP TAENTLVELM RLRNLEAKEV TVRTLSAQGE SVDSSVAAIP
     SDLLVPPSPH PRTAPKSKPL ASAGAPETKE EHLGPHLKID ESWEQTHSAS PVHGHTLEPP
     VPNFPSSLQG RRSPSPNRIL PQPQGTPVPN TVAKAMAREA AQRVAESNRM ERRSVFSERS
     NAAQYANSDD EEDGYDSPNV KRRGASVDDF LKGSELGKQP HYCHGEDYHT ESSRGSDLSD
     IMEEDEEELY SEMQLEDGGR RRVSLTSHNA LKECNKNKTT DATFLEQPDF SQQIHHSKKL
     FSIPEVAEED GEYSELLYKQ GLGMPYKKKS TIARDSRPPR PYNQDQQHNF WYPAKHRISG
     MEDFTADDKG CKYSRSLSRS PDSGLDCGSE EEESRFTFRY TCDSVSANVA SSCCADTADC
     SCRKSMRPLL ARRKTLTRQT SIEEDFGDLG SSFVEPRSEQ VKSSYEKKYE TQKCNRTDNL
     SNEDIQGGWK NDLKMADSRA AGPLAKSSHR DAEDSLLLGN PSSAGRPERV EHAGRRSSHG
     SAVPQRSRPM LVPSIDGYGG HDHLSPDIYE ESETDPGTED ISTRIFVALF DYDPLTMSPN
     PDAAEEELPF KEGQIIKVYG DKDADGFYRG ETCTRIGLIP CNMVSEIQAD DEEMMDQLLK
     QGFLPLNTPV EKIERNRRSG RQHSVSTRRM VALYDYDPRE SSPNVDVEAE LTFCTGDIIT
     VFGEIDEDGF YYGELNGQKG LVPSNFLEEV PDDVEVYLSD APSRYLHDTP MRTKAKRKKS
     VHFTP
 
 
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