RIMB2_MOUSE
ID RIMB2_MOUSE Reviewed; 1072 AA.
AC Q80U40; B9EKT4; E9QPF5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=RIMS-binding protein 2;
DE Short=RIM-BP2;
GN Name=Rimbp2; Synonyms=Kiaa0318, Rbp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-1072 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 735-749, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852; SER-859 AND THR-861, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 RIMS1, RIMS2, CACNA1D and CACNA1B, and
CC potentially with other Ca(2+) channel alpha-1 isoforms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Synapse
CC {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80U40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U40-2; Sequence=VSP_037437;
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; AK044685; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC110566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151100; AAI51101.1; -; mRNA.
DR EMBL; BC151101; AAI51102.1; -; mRNA.
DR EMBL; AK122245; BAC65527.2; -; mRNA.
DR RefSeq; NP_001074857.1; NM_001081388.2.
DR RefSeq; NP_001297662.1; NM_001310733.1.
DR AlphaFoldDB; Q80U40; -.
DR SMR; Q80U40; -.
DR BioGRID; 231164; 2.
DR IntAct; Q80U40; 2.
DR MINT; Q80U40; -.
DR STRING; 10090.ENSMUSP00000106978; -.
DR iPTMnet; Q80U40; -.
DR PhosphoSitePlus; Q80U40; -.
DR MaxQB; Q80U40; -.
DR PaxDb; Q80U40; -.
DR PRIDE; Q80U40; -.
DR ProteomicsDB; 255221; -. [Q80U40-1]
DR ProteomicsDB; 255222; -. [Q80U40-2]
DR Antibodypedia; 65349; 47 antibodies from 13 providers.
DR DNASU; 231760; -.
DR Ensembl; ENSMUST00000199537; ENSMUSP00000143276; ENSMUSG00000029420. [Q80U40-2]
DR GeneID; 231760; -.
DR KEGG; mmu:231760; -.
DR UCSC; uc008zsk.2; mouse. [Q80U40-2]
DR UCSC; uc008zsm.1; mouse. [Q80U40-1]
DR CTD; 23504; -.
DR MGI; MGI:2443235; Rimbp2.
DR VEuPathDB; HostDB:ENSMUSG00000029420; -.
DR eggNOG; KOG3632; Eukaryota.
DR GeneTree; ENSGT00950000183203; -.
DR InParanoid; Q80U40; -.
DR OrthoDB; 102427at2759; -.
DR BioGRID-ORCS; 231760; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rimbp2; mouse.
DR PRO; PR:Q80U40; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80U40; protein.
DR Bgee; ENSMUSG00000029420; Expressed in visual cortex and 101 other tissues.
DR ExpressionAtlas; Q80U40; baseline and differential.
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; IDA:SynGO.
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 Alternative splicing; Cell membrane; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1..1072
FT /note="RIMS-binding protein 2"
FT /id="PRO_0000221384"
FT DOMAIN 181..248
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 311..404
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 407..489
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 503..604
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 868..936
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 972..1039
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 597..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1072
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR1"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIR1"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1065..1072
FT /note="KKSVHFTP -> VSQPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037437"
FT CONFLICT 76
FT /note="E -> Q (in Ref. 1; AK044685)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="A -> V (in Ref. 1; AK044685 and 4; BAC65527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1065
FT /note="Missing (in Ref. 1; AK044685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1072 AA; 118342 MW; 462AD1C103A6CA2E CRC64;
MREAAERRQQ LELEHEQALA FLNAKQQEIQ LLQQAQVEAK KEHEGAVQLL ESKVRELEEK
CRVQSEQFNL LSRDLEKFRQ HTGSIDLLGS SSVALLDVPL APGKPFPQYM NGLATSIHKG
HEGPTGHYSV IGDYIPLSGD KLESPCVKPS FLLRSSSPRC RFESEMDNDR NSNNSKQSSS
GKVHLCVARY SYNPFDGPNE NPEAELPLTA GKYLYVYGDM DEDGFYEGEL LDGQRGLVPS
NFVDFIQDNE SRLAGTLGSE QDQNFLNHSG ISLERDSILH LHSPTQVDSG ITDNGGGTLD
VNIDDIGEDT VPYPRKITLI KQLAKSVIVG WEPPAVPPGW GTVSSYNVLV DKETRMSLAL
GRRTKALIEK LNTAACTYRI SVQCVTSRGN SDELQCTLLV GKDVVVAPSQ LRVDNITQIS
AQLSWLPTNS NYSHIIFLNE EELDIVKAAR YKYQFFNLRP NMAYKVKVLA QPHQMPWQLP
LEQREKKEAC VEFSTLPAGP PAPPQDVTVH AGATAASVQV SWKPPALTPT GLSNGANVTG
YGVYAKGQRV AEVIAPTADG TAVELIRLRS LEAKAVSVRT LSVQGESMDS ALAAIPPDLL
VPPAPHPRTA PPPKPLASDM DTKDQHLGPH VKVDESWEQS RSPGPAHGHM LEPPDMHSAG
PGRRSPSPSR ILPQPQGAPV STTVAKAMAR EAAQRVAESN RLEKRSLFLE QSSAGQYTNS
DEEDGYASPE VKRRGTSVDD FLKGSELGKQ PHCCHGDEYH TESSRGSDLS DIMEEDEEEL
YSEMQLEDGG RRRPSGTSHN ALKILGNSTL MGRADRMEHV SRRYSHSGGG SHRHRPAMAP
SIDEYTGRDH LSPDFYDESE TDPGAEELPA RIFVALFDYD PLTMSPNPDA AEEELPFKEG
QIIKVYGDKD ADGFYRGETC ARLGLIPCNM VSEIHADDEE MMDQLLRQGF LPLNTPVEKI
ERSRRSGRGH SVPTRRMVAL YDYDPRESSP NVDVEAELPF CTGDIITVFG EIDEDGFYYG
ELNGQKGLVP SNFLEEVPDD VEVHLSDAPP HYSHDPPMRS KAKRKKSVHF TP
