RIMB2_RAT
ID RIMB2_RAT Reviewed; 1049 AA.
AC Q9JIR1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=RIMS-binding protein 2;
DE Short=RIM-BP2;
GN Name=Rimbp2; Synonyms=Rbp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 785-1049, AND INTERACTION WITH RIMS1 AND RIMS2.
RX PubMed=10748113; DOI=10.1074/jbc.m909008199;
RA Wang Y., Sugita S., Suedhof T.C.;
RT "The RIM/NIM family of neuronal C2 domain proteins. Interactions with Rab3
RT and a new class of Src homology 3 domain proteins.";
RL J. Biol. Chem. 275:20033-20044(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701; SER-709; SER-832;
RP SER-839 AND THR-841, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in the synaptic transmission as bifunctional
CC linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and
CC CACNA1B. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CACNA1D and CACNA1B, and potentially with other
CC Ca(2+) channel alpha-1 isoforms (By similarity). Interacts with RIMS1
CC and RIMS2. {ECO:0000250, ECO:0000269|PubMed:10748113}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Synapse
CC {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}.
CC -!- DOMAIN: The SH3 domains mediate binding to a proline-rich motif in
CC RIMS1, RIMS2, CACNA1D and CACNA1B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
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DR EMBL; AABR03082106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03082706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03082432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF199336; AAF81658.1; -; mRNA.
DR AlphaFoldDB; Q9JIR1; -.
DR SMR; Q9JIR1; -.
DR CORUM; Q9JIR1; -.
DR IntAct; Q9JIR1; 2.
DR STRING; 10116.ENSRNOP00000059643; -.
DR iPTMnet; Q9JIR1; -.
DR PhosphoSitePlus; Q9JIR1; -.
DR PaxDb; Q9JIR1; -.
DR PRIDE; Q9JIR1; -.
DR RGD; 708533; Rimbp2.
DR eggNOG; KOG3632; Eukaryota.
DR InParanoid; Q9JIR1; -.
DR PRO; PR:Q9JIR1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:RGD.
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; -; 3.
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; 2.
DR PANTHER; PTHR14234:SF18; PTHR14234:SF18; 2.
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; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Synapse.
FT CHAIN 1..1049
FT /note="RIMS-binding protein 2"
FT /id="PRO_0000221385"
FT DOMAIN 164..231
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 294..387
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 390..471
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 486..587
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 848..916
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 952..1019
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 580..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 841
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1049 AA; 115614 MW; 079C513375146B6B CRC64;
MREAAERRQQ LELEHEQALA ILNAKQQEIQ LLQQSKVREL EEKCRVQSEQ FNLLSRDLEK
FRQHAGSIDL LGSNSVALLD VPLAPGKPFS QYMNGLATSI HKGHEGPTGH YSVIGDYIPL
SGDKLESPCV KPSFLLRSSS PRCRFESEMD DDRSSNKSKH SSSGKVHLCV ARYSYNPFDG
PNENPEAELP LTAGKYLYVY GDMDEDGFYE GELLDGQRGL VPSNFVDFIQ DNESRFAGTL
GSEQDQNFLN HSGISLERDS ILHLHSPTQV DSGITDNGGG TLDVNIDDIG EDIVPYPRKI
TLIKQLAKSV IVGWEPPAVP PGWGTVSSYN VLVDKETRMS LALGRRTKAL IEKLNTAACT
YRISVQCVTS RGNSDELQCT LLVGKDVVVA PSQLRVDNIT QISAQLSWLP TNSNYSHIIF
LNEEELDIVK AARYKYQFFN LRPNMAYKVK VLAQPHQMPW QLPLEQREKD EACVEFSTLP
AGPPAPPQDV TVQAGATTAS VQVSWKPPAL TPTGLSNGAN VTGYGVYAKG QRVAEVIAPT
ANGAAVELVR LRSLEAKAVS VRTLSAQGES MDSALAAIPP DLLVPPAPHP RTAPPPKPLT
SDMDTKDLGP HVKVDESWEQ SRPPGPAHGH MLEPPDMHST GPGRRSPSPS RILPQPQGAP
VSTTVAKAMA REAAQRVAET SKLEKRSLFL EQSSAGPYAN SDEEDGYASP EVKRRGTSVD
DFLKGSELGQ QPHCCHGDEY HTESSRGSDL SDIMEEDEEE LYSEMQLEDG GRRRPSGTSH
NALKILGNSA LMGRGDRMEH VSRRYSHSGG GPQRHRPMAP SIDEYTGRDH LSPDFYDESE
TDPGAEELPA RIFVALFDYD PLTMSPNPDA AEEELPFKEG QIIKVYGDKD ADGFYRGETC
ARLGLIPCNM VSEIHADDEE MMDQLLRQGF LPLNTPVEKI ERSRRSGRGH SVPTRRMVAL
YDYDPRESSP NVDVEAELLF CTGDIITVFG EIDEDGFYYG ELNGQKGLVP SNFLEEVPDD
VEVHLSDAPP HYSHDPPMRT KAKRVSQPP
