CIB2_SHEEP
ID CIB2_SHEEP Reviewed; 176 AA.
AC C7A276;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Calcium and integrin-binding family member 2;
DE Flags: Fragment;
GN Name=CIB2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18989754; DOI=10.1007/s11033-008-9383-4;
RA Yu Y., Song X., Du L., Wang C.;
RT "Molecular characterization of the sheep CIB1 gene.";
RL Mol. Biol. Rep. 36:1799-1809(2009).
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. May be involved
CC in the mechanotransduction process. {ECO:0000250,
CC ECO:0000250|UniProtKB:O75838}.
CC -!- SUBUNIT: Homodimer. Interacts with WHRN and MYO7A. Interacts with
CC ITGA2B (via C-terminus cytoplasmic tail region) and ITGA7 (via C-
CC terminus cytoplasmic tail region); the interactions are
CC stabilized/increased in a calcium and magnesium-dependent manner.
CC {ECO:0000250|UniProtKB:O75838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:O75838}. Photoreceptor
CC inner segment {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:Q9Z309}. Cell
CC membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z309}. Note=Colocalized
CC with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular
CC junctions (NMJ). Localizes in the cuticular plate along and at the tip
CC of the stereocilia of vestibular sensory hair cells.
CC {ECO:0000250|UniProtKB:O75838, ECO:0000250|UniProtKB:Q9Z309}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, heart, kidney, brain, spleen,
CC stomach, ovary, testis and muscle (PubMed:18989754).
CC {ECO:0000269|PubMed:18989754}.
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; FJ039530; ACM89972.1; -; mRNA.
DR AlphaFoldDB; C7A276; -.
DR SMR; C7A276; -.
DR STRING; 9940.ENSOARP00000000542; -.
DR eggNOG; KOG0038; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0032437; C:cuticular plate; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; ISS: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 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cell projection; Cytoplasm; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN <1..176
FT /note="Calcium and integrin-binding family member 2"
FT /id="PRO_0000425744"
FT DOMAIN 55..90
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..127
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..168
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 NON_TER 1
SQ SEQUENCE 176 AA; 20459 MW; 47269994F2D04189 CRC64;
LFYRYQDCTF FNKKDILKLH ARFYELAPNL VPMDYRKSPI VHVPMSLIIQ MPELRENPFK
ERIVEAFSED GEGNLTFNDF VDMFSVLCES APRDLKASYA FKIYDFNTDN FICKEDLQLT
LARLTKSELD EDEVVLVCDK VIEEADLDGD GKLGFADFED MIAKAPDFLS TFHIRI
