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Calcium and integrin-binding protein 1 (CIB) (Calmyrin) (DNA-PKcs-interacting protein) (Kinase-interacting protein) (KIP)

 CIB1_MOUSE              Reviewed;         191 AA.
Q9Z0F4; Q3TN80;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 149.
RecName: Full=Calcium and integrin-binding protein 1;
Short=CIB;
AltName: Full=Calmyrin;
AltName: Full=DNA-PKcs-interacting protein;
AltName: Full=Kinase-interacting protein;
Short=KIP;
Name=Cib1; Synonyms=Cib, Kip, Prkdcip;
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=C57BL/6J; TISSUE=Fetal kidney;
PubMed=10051332; DOI=10.1007/s003359900994;
Saito T., Seki N., Hattori A., Hayashi A., Abe M., Araki R.,
Fujimori A., Fukumura R., Kozuma S., Matsuda Y.;
"Structure, expression profile, and chromosomal location of a mouse
gene homologous to human DNA-PKcs interacting protein (KIP) gene.";
Mamm. Genome 10:315-317(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10826701; DOI=10.3109/10425170009015612;
Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.;
"Genomic structure of mouse and human genes for DNA-PKcs interacting
protein (KIP).";
DNA Seq. 10:415-418(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Naik M.U., Naik U.P.;
"Cloning and tissue distribution of murine calcium and integrin
binding protein, CIB.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and 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).
[6]
SUBCELLULAR LOCATION.
PubMed=16418530; DOI=10.1083/jcb.200505131;
Yuan W., Leisner T.M., McFadden A.W., Wang Z., Larson M.K., Clark S.,
Boudignon-Proudhon C., Lam S.C., Parise L.V.;
"CIB1 is an endogenous inhibitor of agonist-induced integrin
alphaIIbbeta3 activation.";
J. Cell Biol. 172:169-175(2006).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16982698; DOI=10.1128/MCB.01488-06;
Yuan W., Leisner T.M., McFadden A.W., Clark S., Hiller S., Maeda N.,
O'Brien D.A., Parise L.V.;
"CIB1 is essential for mouse spermatogenesis.";
Mol. Cell. Biol. 26:8507-8514(2006).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17975111; DOI=10.1161/CIRCRESAHA.107.157586;
Zayed M.A., Yuan W., Leisner T.M., Chalothorn D., McFadden A.W.,
Schaller M.D., Hartnett M.E., Faber J.E., Parise L.V.;
"CIB1 regulates endothelial cells and ischemia-induced pathological
and adaptive angiogenesis.";
Circ. Res. 101:1185-1193(2007).
[9]
INTERACTION WITH MYO1C.
PubMed=17994197; DOI=10.1007/s10974-007-9124-7;
Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M.;
"CIB1 and CaBP1 bind to the myo1c regulatory domain.";
J. Muscle Res. Cell Motil. 28:285-291(2007).
[10]
INTERACTION WITH ITGA2B, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18989529;
Denofrio J.C., Yuan W., Temple B.R., Gentry H.R., Parise L.V.;
"Characterization of calcium- and integrin-binding protein 1 (CIB1)
knockout platelets: potential compensation by CIB family members.";
Thromb. Haemost. 100:847-856(2008).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19691476; DOI=10.1111/j.1538-7836.2009.03581.x;
Naik M.U., Nigam A., Manrai P., Millili P., Czymmek K., Sullivan M.,
Naik U.P.;
"CIB1 deficiency results in impaired thrombosis: the potential role of
CIB1 in outside-in signaling through integrin alpha IIb beta 3.";
J. Thromb. Haemost. 7:1906-1914(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Pancreas, 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).
[13]
FUNCTION.
PubMed=20804551; DOI=10.1186/2040-2384-2-17;
Zayed M.A., Yuan W., Chalothorn D., Faber J.E., Parise L.V.;
"Tumor growth and angiogenesis is impaired in CIB1 knockout mice.";
J. Angiog. Res. 2:17-17(2010).
[14]
INTERACTION WITH CACNA1C AND PPP3R1, SUBCELLULAR LOCATION, INDUCTION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20639889; DOI=10.1038/nm.2181;
Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J.,
Yuan W., Drexler H., Parise L.V., Molkentin J.D.;
"CIB1 is a regulator of pathological cardiac hypertrophy.";
Nat. Med. 16:872-879(2010).
[15]
FUNCTION.
PubMed=22128142; DOI=10.1182/blood-2011-04-346098;
Kostyak J.C., Naik M.U., Naik U.P.;
"Calcium- and integrin-binding protein 1 regulates megakaryocyte
ploidy, adhesion, and migration.";
Blood 119:838-846(2012).
-!- FUNCTION: Calcium-binding protein that plays a role in the
regulation of numerous cellular processes, such as cell
differentiation, cell division, cell proliferation, cell
migration, thrombosis, angiogenesis, cardiac hypertrophy and
apoptosis. Involved in bone marrow megakaryocyte differentiation
by negatively regulating thrombopoietin-mediated signaling
pathway. Participates in the endomitotic cell cycle of
megakaryocyte, a form of mitosis in which both karyokinesis and
cytokinesis are interrupted. Plays a role in integrin signaling by
negatively regulating alpha-IIb/beta3 activation in thrombin-
stimulated megakaryocytes preventing platelet aggregation. Up-
regulates PTK2/FAK1 activity, and is also needed for the
recruitment of PTK2/FAK1 to focal adhesions; it thus appears to
play an important role in focal adhesion formation. Positively
regulates cell migration on fibronectin in a CDC42-dependent
manner, the effect being negatively regulated by PAK1. Functions
as a negative regulator of stress activated MAP kinase (MAPK)
signaling pathways. Down-regulates inositol 1,4,5-trisphosphate
receptor-dependent calcium signaling. Involved in sphingosine
kinase SPHK1 translocation to the plasma membrane in a N-
myristoylation-dependent manner preventing TNF-alpha-induced
apoptosis. Regulates serine/threonine-protein kinase PLK3 activity
for proper completion of cell division progression. Plays a role
in microtubule (MT) dynamics during neuronal development; disrupts
the MT depolymerization activity of STMN2 attenuating NGF-induced
neurite outgrowth and the MT reorganization at the edge of
lamellipodia. Promotes cardiomyocyte hypertrophy via activation of
the calcineurin/NFAT signaling pathway. Stimulates calcineurin
PPP3R1 activity by mediating its anchoring to the sarcolemma. In
ischemia-induced (pathological or adaptive) angiogenesis,
stimulates endothelial cell proliferation, migration and
microvessel formation by activating the PAK1 and ERK1/ERK2
signaling pathway. Promotes also cancer cell survival and
proliferation. May regulate cell cycle and differentiation of
spermatogenic germ cells, and/or differentiation of supporting
Sertoli cells. {ECO:0000269|PubMed:16982698,
ECO:0000269|PubMed:17975111, ECO:0000269|PubMed:19691476,
ECO:0000269|PubMed:20804551, ECO:0000269|PubMed:22128142}.
-!- SUBUNIT: Monomer. Interacts with the heterodimeric integrin alpha-
IIb/beta3 (ITGA2B-ITGB3). Interacts with ITGA2B (via cytoplasmic
domain); the interaction is direct and calcium-dependent.
Interacts with the protein kinases PLK2/SNK and PRKDC (via the
region immediately upstream of the kinase domain). Interacts with
PLK3; the interaction inhibits PLK3 kinase activity. Interacts
with PSEN2. Interacts (via C-terminus) with F8. Interacts with
NBR1 (via C-terminus). Interacts with FEZ1 (via C-terminus).
Interacts with UBR5 (via C-terminus); the interaction is sensitive
to DNA damage, and may target CIB1 for ubiquitin-mediated
degradation. Interacts with IFI6. Interacts with BCL2. Interacts
with TAS1R2 (via C-terminus); the interaction is independent of
the myristoylation state of CIB1. Interacts with ITPR3; the
interaction occurs in a calcium dependent manner. Interacts with
PTK2/FAK1. Interacts with MAP3K5; the interaction inhibits MAP3K5
activation by phosphorylation, and its subsequent interaction with
TRAF2. Interacts (via C-terminal region) with STMN2 (via the N-
terminal region); the interaction is direct, occurs in a calcium-
dependent manner and attenuates the STMN2-induced neurite
outgrowth inhibition. Interacts with SPHK1, the interaction occurs
in a calcium-dependent manner. Interacts with ITGA2B (via C-
terminal cytoplasmic tail); the interaction occurs upon platelet
aggregation and is stabilized/increased in a calcium and
magnesium-dependent manner. Interacts with PAK1 (via N-terminal
region); the interaction is direct and occurs in a calcium-
dependent manner. Interacts with RAC3 (via C-terminal region); the
interaction induces their association with the cytoskeleton upon
alpha-IIb/beta3 integrin-mediated adhesion. Interacts with ITGA5
and ITGAV (By similarity). Interacts with MYO1C. Interacts with
ITGA2B (via C-terminal cytoplasmic tail region). Interacts (via C-
terminal region) with PPP3R1 isoform 1 and isoform 2; the
interactions increase upon cardiomyocytes hypertrophy. Interacts
with CACNA1C; the interaction increases upon cardiomyocytes
hypertrophy. {ECO:0000250, ECO:0000269|PubMed:17994197,
ECO:0000269|PubMed:18989529, ECO:0000269|PubMed:20639889}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}. Cell membrane. Cell membrane, sarcolemma. Cytoplasm
{ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}.
Cytoplasm, perinuclear region {ECO:0000250}. Cell projection,
filopodium tip {ECO:0000250}. Apical cell membrane {ECO:0000250}.
Cell projection, ruffle membrane {ECO:0000250}. Cell projection,
growth cone {ECO:0000250}. Cell projection, lamellipodium
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Note=Colocalized with NBR1 to the perinuclear region (By
similarity). Colocalizes with TAS1R2 in apical regions of taste
receptor cells. Colocalized with RAC3 in the perinuclear area and
at the cell periphery. Colocalized with PAK1 within membrane
ruffles during cell spreading upon readhesion to fibronectin.
Redistributed to the cytoskeleton upon platelet aggregation.
Translocates from the cytosol to the plasma membrane in a calcium-
dependent manner. Colocalized with STMN2 in the cell body,
neurites and growth cones of neurons. Colocalized with STMN2 to
the leading edge of lamellipodia. Colocalizes with PLK3 at the
centrosomes in ductal breast carcinoma cells (By similarity).
Colocalized with PPP3R1 at the cell membrane of cardiomyocytes in
the hypertrophic heart. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in testis. Expressed in cardiac
myocytes and endothelial cells. Expressed strongly in Sertoli
cells, weakly in pachytene spermatocytes, round spermatids and
condensing spermatids (at protein level). Ubiquitous.
{ECO:0000269|PubMed:17975111, ECO:0000269|PubMed:18989529,
ECO:0000269|PubMed:20639889}.
-!- DEVELOPMENTAL STAGE: Expressed in the heart at 16 dpc (at protein
level). {ECO:0000269|PubMed:20639889}.
-!- INDUCTION: Up-regulated upon cardiomyocytes hypertrophy (at
protein level). {ECO:0000269|PubMed:20639889}.
-!- DOMAIN: The EF-hands may also bind magnesium ions in the presence
of high Mg(2+) levels and low Ca(2+) levels. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice grow normally and are healthy; other
family members (CIB2, CIB3 and CIB4) may probably compensate for
CIB1 loss (PubMed:18989529). Males are sterile: spermatogenic
cells can complete both mitotic and meiotic divisions, but
postmeiotic spermatids do not develop normally and sperm is not
produced (PubMed:16982698). Display increased bone marrow
megakaryocytes and circulating platelets (PubMed:22128142). Mice
display tail bleeding time increase, impaired thrombus formation
and angiogenesis defect after ischemia (PubMed:19691476). Show
compromised tumor growth (PubMed:20804551).
{ECO:0000269|PubMed:16982698, ECO:0000269|PubMed:18989529,
ECO:0000269|PubMed:19691476, ECO:0000269|PubMed:20804551,
ECO:0000269|PubMed:22128142}.
-!- MISCELLANEOUS: The binding of either calcium or magnesium
significantly increases the structural stability of the protein in
comparison to apo-CIB (calcium- and magnesium-free form).
{ECO:0000250}.
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EMBL; AB006463; BAA74429.1; -; mRNA.
EMBL; AB017361; BAA36165.1; -; Genomic_DNA.
EMBL; AF173010; AAG38960.1; -; mRNA.
EMBL; AK010345; BAB26868.1; -; mRNA.
EMBL; AK027915; BAC25663.1; -; mRNA.
EMBL; AK152805; BAE31510.1; -; mRNA.
EMBL; AK165472; BAE38209.1; -; mRNA.
EMBL; BC003714; AAH03714.1; -; mRNA.
EMBL; BC054385; AAH54385.1; -; mRNA.
CCDS; CCDS21392.1; -.
RefSeq; NP_001278204.1; NM_001291275.1.
RefSeq; NP_001278205.1; NM_001291276.1.
RefSeq; NP_036000.1; NM_011870.5.
UniGene; Mm.30217; -.
ProteinModelPortal; Q9Z0F4; -.
SMR; Q9Z0F4; -.
STRING; 10090.ENSMUSP00000070901; -.
PhosphoSitePlus; Q9Z0F4; -.
EPD; Q9Z0F4; -.
MaxQB; Q9Z0F4; -.
PaxDb; Q9Z0F4; -.
PeptideAtlas; Q9Z0F4; -.
PRIDE; Q9Z0F4; -.
Ensembl; ENSMUST00000065163; ENSMUSP00000070901; ENSMUSG00000030538.
GeneID; 23991; -.
KEGG; mmu:23991; -.
UCSC; uc009hzs.2; mouse.
CTD; 10519; -.
MGI; MGI:1344418; Cib1.
eggNOG; KOG0034; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00860000133737; -.
HOGENOM; HOG000233019; -.
HOVERGEN; HBG107344; -.
InParanoid; Q9Z0F4; -.
KO; K17259; -.
OMA; QDGDCTF; -.
OrthoDB; EOG091G0OJZ; -.
PhylomeDB; Q9Z0F4; -.
TreeFam; TF313865; -.
PRO; PR:Q9Z0F4; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030538; -.
CleanEx; MM_CIB1; -.
ExpressionAtlas; Q9Z0F4; baseline and differential.
Genevisible; Q9Z0F4; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:HGNC.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:HGNC.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:HGNC.
GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; ISO:MGI.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0043495; F:protein membrane anchor; IMP:BHF-UCL.
GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
GO; GO:0017016; F:Ras GTPase binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; ISS:HGNC.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:HGNC.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
GO; GO:0007113; P:endomitotic cell cycle; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IMP:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:2000256; P:positive regulation of male germ cell proliferation; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IMP:UniProtKB.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
Angiogenesis; Apoptosis; Calcium; Cell adhesion; Cell cycle;
Cell division; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Lipoprotein; Magnesium;
Membrane; Metal-binding; Myristate; Nucleus; Reference proteome;
Repeat; Spermatogenesis.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q99828}.
CHAIN 2 191 Calcium and integrin-binding protein 1.
/FTId=PRO_0000073532.
DOMAIN 103 138 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 148 183 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 116 127 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 161 172 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
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


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