CIB1_MOUSE
ID CIB1_MOUSE Reviewed; 191 AA.
AC Q9Z0F4; Q3TN80;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Calcium and integrin-binding protein 1;
DE Short=CIB;
DE AltName: Full=Calmyrin;
DE AltName: Full=DNA-PKcs-interacting protein;
DE AltName: Full=Kinase-interacting protein;
DE Short=KIP;
GN Name=Cib1; Synonyms=Cib, Kip, Prkdcip;
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=C57BL/6J; TISSUE=Fetal kidney;
RX PubMed=10051332; DOI=10.1007/s003359900994;
RA Saito T., Seki N., Hattori A., Hayashi A., Abe M., Araki R., Fujimori A.,
RA Fukumura R., Kozuma S., Matsuda Y.;
RT "Structure, expression profile, and chromosomal location of a mouse gene
RT homologous to human DNA-PKcs interacting protein (KIP) gene.";
RL Mamm. Genome 10:315-317(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10826701; DOI=10.3109/10425170009015612;
RA Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.;
RT "Genomic structure of mouse and human genes for DNA-PKcs interacting
RT protein (KIP).";
RL DNA Seq. 10:415-418(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Naik M.U., Naik U.P.;
RT "Cloning and tissue distribution of murine calcium and integrin binding
RT protein, CIB.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and 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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16418530; DOI=10.1083/jcb.200505131;
RA Yuan W., Leisner T.M., McFadden A.W., Wang Z., Larson M.K., Clark S.,
RA Boudignon-Proudhon C., Lam S.C., Parise L.V.;
RT "CIB1 is an endogenous inhibitor of agonist-induced integrin alphaIIbbeta3
RT activation.";
RL J. Cell Biol. 172:169-175(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16982698; DOI=10.1128/mcb.01488-06;
RA Yuan W., Leisner T.M., McFadden A.W., Clark S., Hiller S., Maeda N.,
RA O'Brien D.A., Parise L.V.;
RT "CIB1 is essential for mouse spermatogenesis.";
RL Mol. Cell. Biol. 26:8507-8514(2006).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17975111; DOI=10.1161/circresaha.107.157586;
RA Zayed M.A., Yuan W., Leisner T.M., Chalothorn D., McFadden A.W.,
RA Schaller M.D., Hartnett M.E., Faber J.E., Parise L.V.;
RT "CIB1 regulates endothelial cells and ischemia-induced pathological and
RT adaptive angiogenesis.";
RL Circ. Res. 101:1185-1193(2007).
RN [9]
RP INTERACTION WITH MYO1C.
RX PubMed=17994197; DOI=10.1007/s10974-007-9124-7;
RA Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M.;
RT "CIB1 and CaBP1 bind to the myo1c regulatory domain.";
RL J. Muscle Res. Cell Motil. 28:285-291(2007).
RN [10]
RP INTERACTION WITH ITGA2B, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18989529; DOI=10.1160/th08-06-0351;
RA Denofrio J.C., Yuan W., Temple B.R., Gentry H.R., Parise L.V.;
RT "Characterization of calcium- and integrin-binding protein 1 (CIB1)
RT knockout platelets: potential compensation by CIB family members.";
RL Thromb. Haemost. 100:847-856(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19691476; DOI=10.1111/j.1538-7836.2009.03581.x;
RA Naik M.U., Nigam A., Manrai P., Millili P., Czymmek K., Sullivan M.,
RA Naik U.P.;
RT "CIB1 deficiency results in impaired thrombosis: the potential role of CIB1
RT in outside-in signaling through integrin alpha IIb beta 3.";
RL J. Thromb. Haemost. 7:1906-1914(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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 [13]
RP FUNCTION.
RX PubMed=20804551; DOI=10.1186/2040-2384-2-17;
RA Zayed M.A., Yuan W., Chalothorn D., Faber J.E., Parise L.V.;
RT "Tumor growth and angiogenesis is impaired in CIB1 knockout mice.";
RL J. Angiog. Res. 2:17-17(2010).
RN [14]
RP INTERACTION WITH CACNA1C AND PPP3R1, SUBCELLULAR LOCATION, INDUCTION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20639889; DOI=10.1038/nm.2181;
RA Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J., Yuan W.,
RA Drexler H., Parise L.V., Molkentin J.D.;
RT "CIB1 is a regulator of pathological cardiac hypertrophy.";
RL Nat. Med. 16:872-879(2010).
RN [15]
RP FUNCTION.
RX PubMed=22128142; DOI=10.1182/blood-2011-04-346098;
RA Kostyak J.C., Naik M.U., Naik U.P.;
RT "Calcium- and integrin-binding protein 1 regulates megakaryocyte ploidy,
RT adhesion, and migration.";
RL Blood 119:838-846(2012).
CC -!- FUNCTION: Calcium-binding protein that plays a role in the regulation
CC of numerous cellular processes, such as cell differentiation, cell
CC division, cell proliferation, cell migration, thrombosis, angiogenesis,
CC cardiac hypertrophy and apoptosis. Involved in bone marrow
CC megakaryocyte differentiation by negatively regulating thrombopoietin-
CC mediated signaling pathway. Participates in the endomitotic cell cycle
CC of megakaryocyte, a form of mitosis in which both karyokinesis and
CC cytokinesis are interrupted. Plays a role in integrin signaling by
CC negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated
CC megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1
CC activity, and is also needed for the recruitment of PTK2/FAK1 to focal
CC adhesions; it thus appears to play an important role in focal adhesion
CC formation. Positively regulates cell migration on fibronectin in a
CC CDC42-dependent manner, the effect being negatively regulated by PAK1.
CC Functions as a negative regulator of stress activated MAP kinase (MAPK)
CC signaling pathways. Down-regulates inositol 1,4,5-trisphosphate
CC receptor-dependent calcium signaling. Involved in sphingosine kinase
CC SPHK1 translocation to the plasma membrane in a N-myristoylation-
CC dependent manner preventing TNF-alpha-induced apoptosis. Regulates
CC serine/threonine-protein kinase PLK3 activity for proper completion of
CC cell division progression. Plays a role in microtubule (MT) dynamics
CC during neuronal development; disrupts the MT depolymerization activity
CC of STMN2 attenuating NGF-induced neurite outgrowth and the MT
CC reorganization at the edge of lamellipodia. Promotes cardiomyocyte
CC hypertrophy via activation of the calcineurin/NFAT signaling pathway.
CC Stimulates calcineurin PPP3R1 activity by mediating its anchoring to
CC the sarcolemma. In ischemia-induced (pathological or adaptive)
CC angiogenesis, stimulates endothelial cell proliferation, migration and
CC microvessel formation by activating the PAK1 and ERK1/ERK2 signaling
CC pathway. Promotes also cancer cell survival and proliferation. May
CC regulate cell cycle and differentiation of spermatogenic germ cells,
CC and/or differentiation of supporting Sertoli cells.
CC {ECO:0000269|PubMed:16982698, ECO:0000269|PubMed:17975111,
CC ECO:0000269|PubMed:19691476, ECO:0000269|PubMed:20804551,
CC ECO:0000269|PubMed:22128142}.
CC -!- SUBUNIT: Monomer. Interacts with the heterodimeric integrin alpha-
CC IIb/beta3 (ITGA2B-ITGB3). Interacts with ITGA2B (via cytoplasmic
CC domain); the interaction is direct and calcium-dependent. Interacts
CC with the protein kinases PLK2/SNK and PRKDC (via the region immediately
CC upstream of the kinase domain). Interacts with PLK3; the interaction
CC inhibits PLK3 kinase activity. Interacts with PSEN2. Interacts (via C-
CC terminus) with F8. Interacts with NBR1 (via C-terminus). Interacts with
CC FEZ1 (via C-terminus). Interacts with UBR5 (via C-terminus); the
CC interaction is sensitive to DNA damage, and may target CIB1 for
CC ubiquitin-mediated degradation. Interacts with IFI6; the interaction is
CC direct. Interacts with BCL2. Interacts with TAS1R2 (via C-terminus);
CC the interaction is independent of the myristoylation state of CIB1.
CC Interacts with ITPR3; the interaction occurs in a calcium dependent
CC manner. Interacts with PTK2/FAK1. Interacts with MAP3K5; the
CC interaction inhibits MAP3K5 activation by phosphorylation, and its
CC subsequent interaction with TRAF2. Interacts (via C-terminal region)
CC with STMN2 (via the N-terminal region); the interaction is direct,
CC occurs in a calcium-dependent manner and attenuates the STMN2-induced
CC neurite outgrowth inhibition. Interacts with SPHK1, the interaction
CC occurs in a calcium-dependent manner. Interacts with ITGA2B (via C-
CC terminal cytoplasmic tail); the interaction occurs upon platelet
CC aggregation and is stabilized/increased in a calcium and magnesium-
CC dependent manner. Interacts with PAK1 (via N-terminal region); the
CC interaction is direct and occurs in a calcium-dependent manner.
CC Interacts with RAC3 (via C-terminal region); the interaction induces
CC their association with the cytoskeleton upon alpha-IIb/beta3 integrin-
CC mediated adhesion. Interacts with ITGA5 and ITGAV (By similarity).
CC Interacts with MYO1C. Interacts with ITGA2B (via C-terminal cytoplasmic
CC tail region). Interacts (via C-terminal region) with PPP3R1 isoform 1
CC and isoform 2; the interactions increase upon cardiomyocytes
CC hypertrophy. Interacts with CACNA1C; the interaction increases upon
CC cardiomyocytes hypertrophy. Interacts and forms a complex with TMC6 and
CC TMC8 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q99828,
CC ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:18989529,
CC ECO:0000269|PubMed:20639889}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99828}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q99828}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q99828}. Cell membrane
CC {ECO:0000250|UniProtKB:Q99828}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q99828}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q99828}. Cell projection, filopodium tip
CC {ECO:0000250|UniProtKB:Q99828}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q99828}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q99828}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q99828}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q99828}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q99828}. Nucleus
CC {ECO:0000250|UniProtKB:Q99828}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q99828}. Perikaryon
CC {ECO:0000250|UniProtKB:Q99828}. Note=Colocalized with PPP3R1 at the
CC cell membrane of cardiomyocytes in the hypertrophic heart (By
CC similarity). Colocalized with NBR1 to the perinuclear region.
CC Colocalizes with TAS1R2 in apical regions of taste receptor cells.
CC Colocalized with RAC3 in the perinuclear area and at the cell
CC periphery. Colocalized with PAK1 within membrane ruffles during cell
CC spreading upon readhesion to fibronectin. Redistributed to the
CC cytoskeleton upon platelet aggregation. Translocates from the cytosol
CC to the plasma membrane in a calcium-dependent manner. Colocalized with
CC PLK3 at centrosomes in ductal breast carcinoma cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Expressed in cardiac myocytes
CC and endothelial cells. Expressed strongly in Sertoli cells, weakly in
CC pachytene spermatocytes, round spermatids and condensing spermatids (at
CC protein level). Ubiquitous. {ECO:0000269|PubMed:17975111,
CC ECO:0000269|PubMed:18989529, ECO:0000269|PubMed:20639889}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the heart at 16 dpc (at protein
CC level). {ECO:0000269|PubMed:20639889}.
CC -!- INDUCTION: Up-regulated upon cardiomyocytes hypertrophy (at protein
CC level). {ECO:0000269|PubMed:20639889}.
CC -!- DOMAIN: The EF-hands may also bind magnesium ions in the presence of
CC high Mg(2+) levels and low Ca(2+) levels. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice grow normally and are healthy; other family
CC members (CIB2, CIB3 and CIB4) may probably compensate for CIB1 loss
CC (PubMed:18989529). Males are sterile: spermatogenic cells can complete
CC both mitotic and meiotic divisions, but postmeiotic spermatids do not
CC develop normally and sperm is not produced (PubMed:16982698). Display
CC increased bone marrow megakaryocytes and circulating platelets
CC (PubMed:22128142). Mice display tail bleeding time increase, impaired
CC thrombus formation and angiogenesis defect after ischemia
CC (PubMed:19691476). Show compromised tumor growth (PubMed:20804551).
CC {ECO:0000269|PubMed:16982698, ECO:0000269|PubMed:18989529,
CC ECO:0000269|PubMed:19691476, ECO:0000269|PubMed:20804551,
CC ECO:0000269|PubMed:22128142}.
CC -!- MISCELLANEOUS: The binding of either calcium or magnesium significantly
CC increases the structural stability of the protein in comparison to apo-
CC CIB (calcium- and magnesium-free form). {ECO:0000250}.
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DR EMBL; AB006463; BAA74429.1; -; mRNA.
DR EMBL; AB017361; BAA36165.1; -; Genomic_DNA.
DR EMBL; AF173010; AAG38960.1; -; mRNA.
DR EMBL; AK010345; BAB26868.1; -; mRNA.
DR EMBL; AK027915; BAC25663.1; -; mRNA.
DR EMBL; AK152805; BAE31510.1; -; mRNA.
DR EMBL; AK165472; BAE38209.1; -; mRNA.
DR EMBL; BC003714; AAH03714.1; -; mRNA.
DR EMBL; BC054385; AAH54385.1; -; mRNA.
DR CCDS; CCDS21392.1; -.
DR RefSeq; NP_001278204.1; NM_001291275.1.
DR RefSeq; NP_001278205.1; NM_001291276.1.
DR RefSeq; NP_036000.1; NM_011870.5.
DR AlphaFoldDB; Q9Z0F4; -.
DR SMR; Q9Z0F4; -.
DR STRING; 10090.ENSMUSP00000070901; -.
DR PhosphoSitePlus; Q9Z0F4; -.
DR EPD; Q9Z0F4; -.
DR MaxQB; Q9Z0F4; -.
DR PaxDb; Q9Z0F4; -.
DR PeptideAtlas; Q9Z0F4; -.
DR PRIDE; Q9Z0F4; -.
DR ProteomicsDB; 283622; -.
DR Antibodypedia; 28761; 397 antibodies from 34 providers.
DR DNASU; 23991; -.
DR Ensembl; ENSMUST00000065163; ENSMUSP00000070901; ENSMUSG00000030538.
DR GeneID; 23991; -.
DR KEGG; mmu:23991; -.
DR UCSC; uc009hzs.2; mouse.
DR CTD; 10519; -.
DR MGI; MGI:1344418; Cib1.
DR VEuPathDB; HostDB:ENSMUSG00000030538; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000158927; -.
DR HOGENOM; CLU_061288_6_1_1; -.
DR InParanoid; Q9Z0F4; -.
DR OMA; GHNRNAK; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q9Z0F4; -.
DR TreeFam; TF313865; -.
DR BioGRID-ORCS; 23991; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cib1; mouse.
DR PRO; PR:Q9Z0F4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z0F4; protein.
DR Bgee; ENSMUSG00000030538; Expressed in spermatocyte and 256 other tissues.
DR ExpressionAtlas; Q9Z0F4; baseline and differential.
DR Genevisible; Q9Z0F4; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:HGNC-UCL.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:HGNC-UCL.
DR GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:HGNC-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0007113; P:endomitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:2000256; P:positive regulation of male germ cell proliferation; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IMP:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Angiogenesis; Apoptosis; Calcium; Cell adhesion; Cell cycle; Cell division;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Differentiation;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate; Nucleus;
KW Reference proteome; Repeat; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99828"
FT CHAIN 2..191
FT /note="Calcium and integrin-binding protein 1"
FT /id="PRO_0000073532"
FT DOMAIN 103..138
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 148..183
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 21763 MW; C85B603A19F9D9AC CRC64;
MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPP EQRTVEESLH TRVSFEQILS
LPELKANPFK ERICMVFSTS PTRDSLSFED FLDLLSVFSD TATPDIKSHY AFRIFDFDDD
GTLDREDLSQ LVNCLTGEGE DTRLSASEMK QLIDNILEES DIDRDGTINL SEFQHVISRS
PDFASSFKIV L
