ITBP2_MOUSE
ID ITBP2_MOUSE Reviewed; 350 AA.
AC Q9R000; Q9D161;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Integrin beta-1-binding protein 2;
DE AltName: Full=Melusin;
GN Name=Itgb1bp2;
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 [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=10506186; DOI=10.1074/jbc.274.41.29282;
RA Brancaccio M., Guazzone S., Menini N., Sibona E., Hirsch E., De Andrea M.,
RA Rocchi M., Altruda F., Tarone G., Silengo L.;
RT "Melusin is a new muscle-specific interactor for beta(1) integrin
RT cytoplasmic domain.";
RL J. Biol. Chem. 274:29282-29288(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: May play a role during maturation and/or organization of
CC muscles cells.
CC -!- SUBUNIT: Interacts with beta-1 integrin subunit. This interaction is
CC regulated by divalent cations, and it occurs only in absence of
CC calcium.
CC -!- INTERACTION:
CC Q9R000; Q9CS74: Ecd; NbExp=2; IntAct=EBI-7922331, EBI-7922565;
CC Q9R000; P07901: Hsp90aa1; NbExp=5; IntAct=EBI-7922331, EBI-78930;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscles but not
CC in other tissues. Is localized in rows flanking the Z line containing
CC alpha-actinin.
CC -!- DEVELOPMENTAL STAGE: Detectable in embryo limbs at day 15, reached a
CC maximum in newborn, and declined in adult limb muscles. During heart
CC development level remains steady from embryonic day 15 to adult stage.
CC -!- INDUCTION: During muscle regeneration.
CC -!- DOMAIN: The tail domain binds to the cytoplasmic domain of both
CC integrin beta-1a and beta-1d isoforms. The presence of Ca(2+) ions does
CC not prevent binding of a fragment consisting of the second cysteine
CC rich repeat and the tail domain but prevents the binding of the full-
CC length protein.
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DR EMBL; AF140691; AAF01677.1; -; mRNA.
DR EMBL; AK003906; BAB23069.1; -; mRNA.
DR EMBL; BC030035; AAH30035.1; -; mRNA.
DR CCDS; CCDS41079.1; -.
DR RefSeq; NP_038740.1; NM_013712.2.
DR AlphaFoldDB; Q9R000; -.
DR SMR; Q9R000; -.
DR BioGRID; 205012; 7.
DR IntAct; Q9R000; 2.
DR MINT; Q9R000; -.
DR STRING; 10090.ENSMUSP00000033674; -.
DR iPTMnet; Q9R000; -.
DR PhosphoSitePlus; Q9R000; -.
DR MaxQB; Q9R000; -.
DR PaxDb; Q9R000; -.
DR PRIDE; Q9R000; -.
DR ProteomicsDB; 301694; -.
DR Antibodypedia; 13542; 220 antibodies from 29 providers.
DR Ensembl; ENSMUST00000033674; ENSMUSP00000033674; ENSMUSG00000031312.
DR GeneID; 26549; -.
DR KEGG; mmu:26549; -.
DR UCSC; uc009txu.1; mouse.
DR CTD; 26548; -.
DR MGI; MGI:1353420; Itgb1bp2.
DR VEuPathDB; HostDB:ENSMUSG00000031312; -.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000159429; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; Q9R000; -.
DR OMA; TVRNDFY; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9R000; -.
DR TreeFam; TF105394; -.
DR BioGRID-ORCS; 26549; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q9R000; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R000; protein.
DR Bgee; ENSMUSG00000031312; Expressed in interventricular septum and 106 other tissues.
DR Genevisible; Q9R000; MM.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHORD_protein.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; PTHR12621; 1.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Repeat; SH3-binding; Zinc.
FT CHAIN 1..350
FT /note="Integrin beta-1-binding protein 2"
FT /id="PRO_0000084268"
FT DOMAIN 5..64
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 150..209
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 216..305
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 28..31
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 70..79
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 159..162
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 173..176
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 235..238
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..350
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT CONFLICT 148
FT /note="S -> F (in Ref. 2; BAB23069)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="H -> Y (in Ref. 2; BAB23069)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..189
FT /note="MKSWSCCG -> KKFLKLLC (in Ref. 2; BAB23069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38768 MW; 6DEBCCF805DE9289 CRC64;
MSLLCYNKGC GQHFDPNTNL PDSCRYHPGV PIFHDALKGW SCCRKRTVDF SEFLNIKGCT
VGLHCAEKLP EVPPQPEGPA TSSLQEQKPL NTIPKSAETL FRERPKSEMP PKLLPLLISQ
ALGVALEQKE LDQEPGAGLD NSLIWTGSSC QNPGCDAVYQ GPESDATPCT YHPGAPRFHE
GMKSWSCCGI QTLDFGAFLA QPGCRVGRHD WAKQLPASCR HDWHQTDSVV VLTVYGQIPL
PAFNWVKASQ TELHVHIVFD GNRVFQAQMK LWGVINVEQS SVSLMPSRVE ISLVKADPGS
WAQLEHPDSL AEKARAGVLL EMDEEESEDS DDDLSWTEEE DEEEEEAMGE
