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Integrin beta-1-binding protein 1 (Bodenin)

 ITBP1_MOUSE             Reviewed;         200 AA.
O35671; Q542A8;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-APR-2018, entry version 120.
RecName: Full=Integrin beta-1-binding protein 1;
AltName: Full=Bodenin;
Name=Itgb1bp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=9626504;
DOI=10.1002/(SICI)1097-0177(199806)212:2<293::AID-AJA14>3.0.CO;2-5;
Faisst A.M., Gruss P.;
"Bodenin: a novel murine gene expressed in restricted areas of the
brain.";
Dev. Dyn. 212:293-303(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH ROCK1, AND SUBCELLULAR LOCATION.
PubMed=16741948; DOI=10.1002/jcp.20699;
Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D.,
Jalink K., Roos E.;
"Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts
with the ROCK-I kinase at the plasma membrane.";
J. Cell. Physiol. 208:620-628(2006).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17567669; DOI=10.1242/dev.000877;
Bouvard D., Aszodi A., Kostka G., Block M.R., Albiges-Rizo C.,
Fassler R.;
"Defective osteoblast function in ICAP-1-deficient mice.";
Development 134:2615-2625(2007).
[6]
FUNCTION.
PubMed=18227284; DOI=10.1083/jcb.200707142;
Millon-Fremillon A., Bouvard D., Grichine A., Manet-Dupe S.,
Block M.R., Albiges-Rizo C.;
"Cell adaptive response to extracellular matrix density is controlled
by ICAP-1-dependent beta1-integrin affinity.";
J. Cell Biol. 180:427-441(2008).
[7]
FUNCTION, AND INTERACTION WITH ROCK1.
PubMed=17654484; DOI=10.1002/jcp.21215;
Alvarez B., Stroeken P.J., Edel M.J., Roos E.;
"Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes
migration of myoblasts and affects focal adhesions.";
J. Cell. Physiol. 214:474-482(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION.
PubMed=21768292; DOI=10.1083/jcb.201007108;
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
fibronectin deposition.";
J. Cell Biol. 194:307-322(2011).
-!- FUNCTION: Key regulator of the integrin-mediated cell-matrix
interaction signaling by binding to the ITGB1 cytoplasmic tail and
preventing the activation of integrin alpha-5/beta-1 (heterodimer
of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell
proliferation, differentiation, spreading, adhesion and migration
in the context of mineralization and bone development and
angiogenesis. Stimulates cellular proliferation in a fibronectin-
dependent manner. Involved in the regulation of beta-1 integrin-
containing focal adhesion (FA) site dynamics by controlling its
assembly rate during cell adhesion; inhibits beta-1 integrin
clustering within FA by directly competing with talin TLN1, and
hence stimulates osteoblast spreading and migration in a
fibronectin-and/or collagen-dependent manner. Acts as a guanine
nucleotide dissociation inhibitor (GDI) by regulating Rho family
GTPases during integrin-mediated cell matrix adhesion; reduces the
level of active GTP-bound form of both CDC42 and RAC1 GTPases upon
cell adhesion to fibronectin. Stimulates the release of active
CDC42 from the membranes to maintain it in an inactive cytoplasmic
pool. Participates in the translocation of the Rho-associated
protein kinase ROCK1 to membrane ruffles at cell leading edges of
the cell membrane, leading to an increase of myoblast cell
migration on laminin. Plays a role in bone mineralization at a
late stage of osteoblast differentiation; modulates the dynamic
formation of focal adhesions into fibrillar adhesions, which are
adhesive structures responsible for fibronectin deposition and
fibrillogenesis. Plays a role in blood vessel development; acts as
a negative regulator of angiogenesis by attenuating endothelial
cell proliferation and migration, lumen formation and sprouting
angiogenesis by promoting AKT phosphorylation and inhibiting
ERK1/2 phosphorylation through activation of the Notch signaling
pathway. Promotes transcriptional activity of the MYC promoter.
{ECO:0000269|PubMed:16741948, ECO:0000269|PubMed:17567669,
ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:18227284,
ECO:0000269|PubMed:21768292}.
-!- SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1
and RAP1A. Interacts (via C-terminal region) with ITGB1 (via C-
terminal cytoplasmic tail); the interaction prevents talin TLN1
binding to ITGB1 and KRIT1 and ITGB1 compete for the same binding
site. Interacts with KRIT1 (via N-terminal NPXY motif); the
interaction induces the opening conformation of KRIT1 and KRIT1
and ITGB1 compete for the same binding site. Isoform 2 does not
interact with ITGB1. Interacts with CDC42 (GTP- or GDP-bound
form); the interaction is increased with the CDC42-membrane bound
forms and prevents both CDC42 activation and cell spreading.
Interacts (via C-terminal domain region) with NME2. Interacts with
FERMT2 and RAC1 (By similarity). Interacts (via N-terminus and PTB
domain) with ROCK1. {ECO:0000250, ECO:0000269|PubMed:16741948,
ECO:0000269|PubMed:17654484}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:16741948}. Cell membrane
{ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium
{ECO:0000269|PubMed:16741948}. Cell projection, ruffle
{ECO:0000269|PubMed:16741948}. Note=Nucleocytoplasmic shuttling
protein; shuttles between nucleus and cytoplasm in a integrin-
dependent manner; probably sequestered in the cytosol by ITGB1.
Its localization is dependent on the stage of cell spreading on
fibronectin; cytoplasmic in case of round cells, corresponding to
the initial step of cell spreading, or nuclear in case of well
spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin
engagement sites. Together with ITGB1 and NME2 is recruited to
beta-1 integrin-rich peripheral ruffles and lamellipodia during
initial cell spreading on fibronectin and/or collagen (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the brain.
-!- DEVELOPMENTAL STAGE: First expressed in the heart primordium at
E8.5.
-!- PTM: Phosphorylation at Thr-38 seems to enhance integrin
alpha5beta1-mediated cell adhesion. The degree of phosphorylation
is regulated by integrin-dependent cell-matrix interaction (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show severe defects in osteoblast
mesenchymal cells to compaction, proliferation, differentiation,
and mineralization and to a delay in bone nodule formation. Suffer
also from an excessive microvessel growth.
{ECO:0000269|PubMed:17567669}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ001373; CAA04706.1; -; mRNA.
EMBL; AK002786; BAB22357.1; -; mRNA.
EMBL; AK004172; BAB23206.1; -; mRNA.
EMBL; AK007635; BAB25151.1; -; mRNA.
EMBL; AK075577; BAC35832.1; -; mRNA.
EMBL; AK089937; BAC41007.1; -; mRNA.
EMBL; BC028772; AAH28772.1; -; mRNA.
CCDS; CCDS25833.1; -.
RefSeq; NP_032429.1; NM_008403.4.
RefSeq; XP_006515054.1; XM_006514991.3.
UniGene; Mm.273333; -.
ProteinModelPortal; O35671; -.
SMR; O35671; -.
STRING; 10090.ENSMUSP00000075609; -.
iPTMnet; O35671; -.
PhosphoSitePlus; O35671; -.
EPD; O35671; -.
MaxQB; O35671; -.
PaxDb; O35671; -.
PRIDE; O35671; -.
Ensembl; ENSMUST00000076260; ENSMUSP00000075609; ENSMUSG00000062352.
Ensembl; ENSMUST00000173729; ENSMUSP00000134627; ENSMUSG00000062352.
GeneID; 16413; -.
KEGG; mmu:16413; -.
UCSC; uc007ndl.1; mouse.
CTD; 9270; -.
MGI; MGI:1306802; Itgb1bp1.
eggNOG; ENOG410IFN6; Eukaryota.
eggNOG; ENOG4111GWT; LUCA.
GeneTree; ENSGT00390000003990; -.
HOGENOM; HOG000015089; -.
HOVERGEN; HBG052155; -.
InParanoid; O35671; -.
KO; K20058; -.
OMA; RMLCYDD; -.
OrthoDB; EOG091G16AY; -.
PhylomeDB; O35671; -.
TreeFam; TF105393; -.
PRO; PR:O35671; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000062352; -.
CleanEx; MM_ITGB1BP1; -.
ExpressionAtlas; O35671; baseline and differential.
Genevisible; O35671; MM.
GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:HGNC.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0008565; F:protein transporter activity; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007160; P:cell-matrix adhesion; ISS:HGNC.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
GO; GO:0033622; P:integrin activation; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IDA:UniProtKB.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; ISS:UniProtKB.
GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035148; P:tube formation; ISS:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019517; Integrin-bd_ICAP-1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
PANTHER; PTHR32055; PTHR32055; 1.
Pfam; PF10480; ICAP-1_inte_bdg; 1.
SMART; SM00462; PTB; 1.
1: Evidence at protein level;
Angiogenesis; Biomineralization; Cell adhesion; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Membrane; Mitogen; Notch signaling pathway; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 200 Integrin beta-1-binding protein 1.
/FTId=PRO_0000084265.
DOMAIN 58 200 PID.
REGION 136 139 Interaction with KRIT1. {ECO:0000250}.
REGION 139 141 Interaction with ITGB1. {ECO:0000250}.
MOTIF 6 7 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 10 55 Ser/Thr-rich.
MOD_RES 38 38 Phosphothreonine; by CaMK2.
{ECO:0000250|UniProtKB:O14713}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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


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