ID   M126_CHICK              Reviewed;         119 AA.
AC   P28318;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein MRP-126;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn; TISSUE=Bone marrow;
RX   PubMed=1549365;
RA   Nakano T., Graf T.;
RT   "Identification of genes differentially expressed in two types of v-myb-
RT   transformed avian myelomonocytic cells.";
RL   Oncogene 7:527-534(1992).
CC   -!- TISSUE SPECIFICITY: Expressed in v-myb-transformed myelomonocytic
CC       cells.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; X61200; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001292080.1; NM_001305151.1.
DR   AlphaFoldDB; P28318; -.
DR   SMR; P28318; -.
DR   STRING; 9031.ENSGALP00000022671; -.
DR   PaxDb; P28318; -.
DR   Ensembl; ENSGALT00000022711; ENSGALP00000022671; ENSGALG00000024272.
DR   GeneID; 426356; -.
DR   KEGG; gga:426356; -.
DR   CTD; 6283; -.
DR   VEuPathDB; HostDB:geneid_426356; -.
DR   eggNOG; ENOG502SA01; Eukaryota.
DR   GeneTree; ENSGT00940000162189; -.
DR   HOGENOM; CLU_138624_6_0_1; -.
DR   InParanoid; P28318; -.
DR   OMA; HEHLHFC; -.
DR   OrthoDB; 1521098at2759; -.
DR   PhylomeDB; P28318; -.
DR   TreeFam; TF332727; -.
DR   Reactome; R-GGA-5668599; RHO GTPases Activate NADPH Oxidases.
DR   Reactome; R-GGA-5686938; Regulation of TLR by endogenous ligand.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   Reactome; R-GGA-6799990; Metal sequestration by antimicrobial proteins.
DR   PRO; PR:P28318; -.
DR   Proteomes; UP000000539; Chromosome 25.
DR   Bgee; ENSGALG00000024272; Expressed in granulocyte and 8 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..119
FT                   /note="Protein MRP-126"
FT                   /id="PRO_0000144025"
FT   DOMAIN          23..58
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          59..94
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         42
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   119 AA;  14065 MW;  2D268DAF6309AD7A CRC64;
     MSKGCQTQGP LSELEKAIDV IIDVFHQYSR REGDKDTLTR KELKLLIEKQ LANYLKHVKN
     QVSIDQIFKD LDNNKDQQLS FGEVMLLIIR VTVATHEHLH FCEDHQQQHQ HQHQHQHNH