CIB2_MOUSE
ID CIB2_MOUSE Reviewed; 187 AA.
AC Q9Z309;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Calcium and integrin-binding family member 2;
DE AltName: Full=Kinase-interacting protein 2;
DE Short=KIP 2;
GN Name=Cib2; Synonyms=Kip2;
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=Brain, and Testis;
RX PubMed=9931475; DOI=10.1016/s0167-4781(98)00253-x;
RA Seki N., Hattori A., Hayashi A., Kozuma S., Ohira M., Hori T., Saito T.;
RT "Structure, expression profile and chromosomal location of an isolog of
RT DNA-PKcs interacting protein (KIP) gene.";
RL Biochim. Biophys. Acta 1444:143-147(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [3]
RP INTERACTION WITH ITGA7, CALCIUM-BINDING, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18611855; DOI=10.1074/jbc.m801166200;
RA Hager M., Bigotti M.G., Meszaros R., Carmignac V., Holmberg J.,
RA Allamand V., Akerlund M., Kalamajski S., Brancaccio A., Mayer U.,
RA Durbeej M.;
RT "Cib2 binds integrin alpha7Bbeta1D and is reduced in laminin alpha2 chain-
RT deficient muscular dystrophy.";
RL J. Biol. Chem. 283:24760-24769(2008).
RN [4]
RP INTERACTION WITH ITGA2B, 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23023331; DOI=10.1038/ng.2426;
RA Riazuddin S., Belyantseva I.A., Giese A.P., Lee K., Indzhykulian A.A.,
RA Nandamuri S.P., Yousaf R., Sinha G.P., Lee S., Terrell D., Hegde R.S.,
RA Ali R.A., Anwar S., Andrade-Elizondo P.B., Sirmaci A., Parise L.V.,
RA Basit S., Wali A., Ayub M., Ansar M., Ahmad W., Khan S.N., Akram J.,
RA Tekin M., Riazuddin S., Cook T., Buschbeck E.K., Frolenkov G.I., Leal S.M.,
RA Friedman T.B., Ahmed Z.M.;
RT "Alterations of the CIB2 calcium- and integrin-binding protein cause Usher
RT syndrome type 1J and nonsyndromic deafness DFNB48.";
RL Nat. Genet. 44:1265-1271(2012).
CC -!- FUNCTION: Calcium-binding protein critical for proper photoreceptor
CC cell maintenance and function. Plays a role in intracellular calcium
CC homeostasis by decreasing ATP-induced calcium release
CC (PubMed:23023331). May be involved in the mechanotransduction process
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:23023331}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with WHRN and MYO7A (By
CC similarity). Interacts with ITGA2B (via C-terminus cytoplasmic tail
CC region); this interaction is stabilized/increased in a calcium and
CC magnesium-dependent manner (PubMed:18611855). Interacts with ITGA7 (via
CC C-terminus cytoplasmic tail region); this interaction is
CC stabilized/increased in a calcium and magnesium-dependent manner
CC (PubMed:18989529). {ECO:0000250|UniProtKB:O75838,
CC ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:18989529}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23023331}. Cell
CC projection, stereocilium {ECO:0000269|PubMed:23023331}. Photoreceptor
CC inner segment {ECO:0000269|PubMed:23023331}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:23023331}. Cell
CC membrane, sarcolemma {ECO:0000269|PubMed:18611855}. Note=Colocalized
CC with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular
CC junctions (NMJ) (PubMed:18611855). Localizes in the cuticular plate
CC along and at the tip of the stereocilia of vestibular sensory hair
CC cells (By similarity). {ECO:0000250|UniProtKB:O75838,
CC ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:23023331}.
CC -!- TISSUE SPECIFICITY: Expressed in the supporting cells in both the organ
CC of Corti and the vestibular sensory epithelia. Expressed in inner and
CC outer segments of photoreceptor cells, as well as in the pigmented
CC epithelium. Also observed in the inner and outer plexiform layers and
CC in the ganglion cell layer (at protein level) (PubMed:23023331). Widely
CC expressed (PubMed:23023331). Strongly expressed in skeletal muscles,
CC brain, kidney and liver (PubMed:23023331). Also expressed in the
CC skeletal muscle, retina and cochlea (PubMed:18611855, PubMed:23023331).
CC Expressed in megakaryocytes and endothelial cells (PubMed:18989529).
CC {ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:18989529,
CC ECO:0000269|PubMed:23023331}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the central nervous system and in
CC muscle at 16 dpc, onward (PubMed:18611855). Expressed in the inner ear
CC and retina at 15.5 and 17.5 dpc (PubMed:23023331).
CC {ECO:0000269|PubMed:18611855, ECO:0000269|PubMed:23023331}.
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|UniProtKB:O75838}.
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DR EMBL; AB016080; BAA36545.1; -; mRNA.
DR EMBL; BC005739; AAH05739.1; -; mRNA.
DR CCDS; CCDS40642.1; -.
DR RefSeq; NP_062660.1; NM_019686.5.
DR AlphaFoldDB; Q9Z309; -.
DR SMR; Q9Z309; -.
DR STRING; 10090.ENSMUSP00000038527; -.
DR PhosphoSitePlus; Q9Z309; -.
DR PaxDb; Q9Z309; -.
DR PRIDE; Q9Z309; -.
DR Antibodypedia; 14987; 206 antibodies from 28 providers.
DR DNASU; 56506; -.
DR Ensembl; ENSMUST00000041901; ENSMUSP00000038527; ENSMUSG00000037493.
DR GeneID; 56506; -.
DR KEGG; mmu:56506; -.
DR UCSC; uc009prf.1; mouse.
DR CTD; 10518; -.
DR MGI; MGI:1929293; Cib2.
DR VEuPathDB; HostDB:ENSMUSG00000037493; -.
DR eggNOG; KOG0038; Eukaryota.
DR GeneTree; ENSGT00940000157327; -.
DR HOGENOM; CLU_061288_6_0_1; -.
DR InParanoid; Q9Z309; -.
DR OMA; RYYEMAP; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q9Z309; -.
DR TreeFam; TF313865; -.
DR BioGRID-ORCS; 56506; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cib2; mouse.
DR PRO; PR:Q9Z309; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z309; protein.
DR Bgee; ENSMUSG00000037493; Expressed in hindlimb stylopod muscle and 178 other tissues.
DR ExpressionAtlas; Q9Z309; baseline and differential.
DR Genevisible; Q9Z309; MM.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0032437; C:cuticular plate; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005927; C:muscle tendon junction; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS: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; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Cytoplasm; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..187
FT /note="Calcium and integrin-binding family member 2"
FT /id="PRO_0000073535"
FT DOMAIN 66..101
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 103..138
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 3"
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 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 187 AA; 21704 MW; D21D21DCBD0B6F5C CRC64;
MGNKQTIFTE EQLDNYQDCT FFNKKDILKL HARFYELAPN LVPMDYRKSP IVHVPMSLII
QMPELRENPF KERIVEAFSE DGEGNLTFND FVDMFSVLCE SAPRELKANY AFKIYDFNTD
NFICKEDLEM TLARLTKSEL EEDEVVLVCD KVIEEADLDG DGKLGFADFE DMIAKAPDFL
STFHIRI
