ITBP1_MOUSE
ID ITBP1_MOUSE Reviewed; 200 AA.
AC O35671; Q542A8;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Integrin beta-1-binding protein 1;
DE AltName: Full=Bodenin;
GN Name=Itgb1bp1;
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 STRAIN=BALB/cJ;
RX PubMed=9626504;
RX DOI=10.1002/(sici)1097-0177(199806)212:2<293::aid-aja14>3.0.co;2-5;
RA Faisst A.M., Gruss P.;
RT "Bodenin: a novel murine gene expressed in restricted areas of the brain.";
RL Dev. Dyn. 212:293-303(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Pancreas;
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 FUNCTION, INTERACTION WITH ROCK1, AND SUBCELLULAR LOCATION.
RX PubMed=16741948; DOI=10.1002/jcp.20699;
RA Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D.,
RA Jalink K., Roos E.;
RT "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with
RT the ROCK-I kinase at the plasma membrane.";
RL J. Cell. Physiol. 208:620-628(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17567669; DOI=10.1242/dev.000877;
RA Bouvard D., Aszodi A., Kostka G., Block M.R., Albiges-Rizo C., Fassler R.;
RT "Defective osteoblast function in ICAP-1-deficient mice.";
RL Development 134:2615-2625(2007).
RN [6]
RP FUNCTION.
RX PubMed=18227284; DOI=10.1083/jcb.200707142;
RA Millon-Fremillon A., Bouvard D., Grichine A., Manet-Dupe S., Block M.R.,
RA Albiges-Rizo C.;
RT "Cell adaptive response to extracellular matrix density is controlled by
RT ICAP-1-dependent beta1-integrin affinity.";
RL J. Cell Biol. 180:427-441(2008).
RN [7]
RP FUNCTION, AND INTERACTION WITH ROCK1.
RX PubMed=17654484; DOI=10.1002/jcp.21215;
RA Alvarez B., Stroeken P.J., Edel M.J., Roos E.;
RT "Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes
RT migration of myoblasts and affects focal adhesions.";
RL J. Cell. Physiol. 214:474-482(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
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).
RN [9]
RP FUNCTION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
CC -!- FUNCTION: Key regulator of the integrin-mediated cell-matrix
CC interaction signaling by binding to the ITGB1 cytoplasmic tail and
CC preventing the activation of integrin alpha-5/beta-1 (heterodimer of
CC ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell
CC proliferation, differentiation, spreading, adhesion and migration in
CC the context of mineralization and bone development and angiogenesis.
CC Stimulates cellular proliferation in a fibronectin-dependent manner.
CC Involved in the regulation of beta-1 integrin-containing focal adhesion
CC (FA) site dynamics by controlling its assembly rate during cell
CC adhesion; inhibits beta-1 integrin clustering within FA by directly
CC competing with talin TLN1, and hence stimulates osteoblast spreading
CC and migration in a fibronectin- and/or collagen-dependent manner. Acts
CC as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho
CC family GTPases during integrin-mediated cell matrix adhesion; reduces
CC the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon
CC cell adhesion to fibronectin. Stimulates the release of active CDC42
CC from the membranes to maintain it in an inactive cytoplasmic pool.
CC Participates in the translocation of the Rho-associated protein kinase
CC ROCK1 to membrane ruffles at cell leading edges of the cell membrane,
CC leading to an increase of myoblast cell migration on laminin. Plays a
CC role in bone mineralization at a late stage of osteoblast
CC differentiation; modulates the dynamic formation of focal adhesions
CC into fibrillar adhesions, which are adhesive structures responsible for
CC fibronectin deposition and fibrillogenesis. Plays a role in blood
CC vessel development; acts as a negative regulator of angiogenesis by
CC attenuating endothelial cell proliferation and migration, lumen
CC formation and sprouting angiogenesis by promoting AKT phosphorylation
CC and inhibiting ERK1/2 phosphorylation through activation of the Notch
CC signaling pathway. Promotes transcriptional activity of the MYC
CC promoter. {ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17567669,
CC ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:18227284,
CC ECO:0000269|PubMed:21768292}.
CC -!- SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and
CC RAP1A. Interacts (via C-terminal region) with ITGB1 (via C-terminal
CC cytoplasmic tail); the interaction prevents talin TLN1 binding to ITGB1
CC and KRIT1 and ITGB1 compete for the same binding site. Interacts with
CC KRIT1 (via N-terminal NPXY motif); the interaction induces the opening
CC conformation of KRIT1 and KRIT1 and ITGB1 compete for the same binding
CC site. Isoform 2 does not interact with ITGB1. Interacts with CDC42
CC (GTP- or GDP-bound form); the interaction is increased with the CDC42-
CC membrane bound forms and prevents both CDC42 activation and cell
CC spreading. Interacts (via C-terminal domain region) with NME2.
CC Interacts with FERMT2 and RAC1 (By similarity). Interacts (via N-
CC terminus and PTB domain) with ROCK1. {ECO:0000250,
CC ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17654484}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16741948}. Cell membrane
CC {ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:16741948}. Cell projection, ruffle
CC {ECO:0000269|PubMed:16741948}. Note=Nucleocytoplasmic shuttling
CC protein; shuttles between nucleus and cytoplasm in an integrin-
CC dependent manner; probably sequestered in the cytosol by ITGB1. Its
CC localization is dependent on the stage of cell spreading on
CC fibronectin; cytoplasmic in case of round cells, corresponding to the
CC initial step of cell spreading, or nuclear in case of well spread
CC cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement
CC sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-
CC rich peripheral ruffles and lamellipodia during initial cell spreading
CC on fibronectin and/or collagen (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC -!- DEVELOPMENTAL STAGE: First expressed in the heart primordium at 8.5
CC dpc.
CC -!- PTM: Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-
CC mediated cell adhesion. The degree of phosphorylation is regulated by
CC integrin-dependent cell-matrix interaction (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show severe defects in osteoblast
CC mesenchymal cells to compaction, proliferation, differentiation, and
CC mineralization and to a delay in bone nodule formation. Suffer also
CC from an excessive microvessel growth. {ECO:0000269|PubMed:17567669}.
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DR EMBL; AJ001373; CAA04706.1; -; mRNA.
DR EMBL; AK002786; BAB22357.1; -; mRNA.
DR EMBL; AK004172; BAB23206.1; -; mRNA.
DR EMBL; AK007635; BAB25151.1; -; mRNA.
DR EMBL; AK075577; BAC35832.1; -; mRNA.
DR EMBL; AK089937; BAC41007.1; -; mRNA.
DR EMBL; BC028772; AAH28772.1; -; mRNA.
DR CCDS; CCDS25833.1; -.
DR RefSeq; NP_032429.1; NM_008403.4.
DR RefSeq; XP_006515054.1; XM_006514991.3.
DR AlphaFoldDB; O35671; -.
DR SMR; O35671; -.
DR BioGRID; 200827; 1.
DR IntAct; O35671; 1.
DR MINT; O35671; -.
DR STRING; 10090.ENSMUSP00000075609; -.
DR iPTMnet; O35671; -.
DR PhosphoSitePlus; O35671; -.
DR EPD; O35671; -.
DR jPOST; O35671; -.
DR MaxQB; O35671; -.
DR PaxDb; O35671; -.
DR PRIDE; O35671; -.
DR ProteomicsDB; 269104; -.
DR Antibodypedia; 26528; 223 antibodies from 28 providers.
DR DNASU; 16413; -.
DR Ensembl; ENSMUST00000076260; ENSMUSP00000075609; ENSMUSG00000062352.
DR Ensembl; ENSMUST00000173729; ENSMUSP00000134627; ENSMUSG00000062352.
DR Ensembl; ENSMUST00000232072; ENSMUSP00000156312; ENSMUSG00000062352.
DR GeneID; 16413; -.
DR KEGG; mmu:16413; -.
DR UCSC; uc007ndl.1; mouse.
DR CTD; 9270; -.
DR MGI; MGI:1306802; Itgb1bp1.
DR VEuPathDB; HostDB:ENSMUSG00000062352; -.
DR eggNOG; ENOG502QS6V; Eukaryota.
DR GeneTree; ENSGT00390000003990; -.
DR HOGENOM; CLU_117247_0_0_1; -.
DR InParanoid; O35671; -.
DR OMA; QCHSLEQ; -.
DR OrthoDB; 1409828at2759; -.
DR PhylomeDB; O35671; -.
DR TreeFam; TF105393; -.
DR BioGRID-ORCS; 16413; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Itgb1bp1; mouse.
DR PRO; PR:O35671; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35671; protein.
DR Bgee; ENSMUSG00000062352; Expressed in seminiferous tubule of testis and 259 other tissues.
DR ExpressionAtlas; O35671; baseline and differential.
DR Genevisible; O35671; MM.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISS:UniProtKB.
DR GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:HGNC-UCL.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0033622; P:integrin activation; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IDA:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR InterPro; IPR019517; Integrin-bd_ICAP-1.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR32055; PTHR32055; 1.
DR Pfam; PF10480; ICAP-1_inte_bdg; 1.
DR SMART; SM00462; PTB; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Biomineralization; Cell adhesion; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Differentiation; Membrane;
KW Mitogen; Notch signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..200
FT /note="Integrin beta-1-binding protein 1"
FT /id="PRO_0000084265"
FT DOMAIN 58..200
FT /note="PID"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..139
FT /note="Interaction with KRIT1"
FT /evidence="ECO:0000250"
FT REGION 139..141
FT /note="Interaction with ITGB1"
FT /evidence="ECO:0000250"
FT MOTIF 6..7
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 12..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphothreonine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:O14713"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 200 AA; 21644 MW; F7F0EB09490AEA37 CRC64;
MFRKGKKRHS SSSSQSSEIS TKSKSVDSSL GGLSRSSTVA SLDTDSTKSS GQSNSNLDTC
AEFRIKYVGA IEKLAVSEGK SLEGPLDLIN YIDVAQQDGK LPFVPLEEEF ILGVSKYGIK
VSTTDQHGVL HRHALYLIIR MVCYDDGLGA GKSLLALKTT DASNEEYSLW VYQCNSLEQA
QAICKVLSTA FDSVLTSDKS
