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HBBC_CAPHI
ID   HBBC_CAPHI              Reviewed;         142 AA.
AC   P02078; Q28326;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Hemoglobin subunit beta-C;
DE   AltName: Full=Beta-C-globin;
DE   AltName: Full=Cysteine beta-globin;
DE   AltName: Full=Hemoglobin beta-C chain;
GN   Name=HBBC;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6277503; DOI=10.1016/0092-8674(81)90419-0;
RA   Schon E.A., Cleary M.L., Haynes J.R., Lingrel J.B.;
RT   "Structure and evolution of goat gamma-, beta C- and beta A-globin genes:
RT   three developmentally regulated genes contain inserted elements.";
RL   Cell 27:359-369(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-135.
RX   PubMed=6248519; DOI=10.1016/s0021-9258(18)43745-3;
RA   Haynes J.R., Rosteck P.R. Jr., Schon E.A., Gallagher P.M., Burks D.J.,
RA   Smith K., Lingrel J.B.;
RT   "The isolation of the beta A-, beta C-, and gamma-globin genes and a
RT   presumptive embryonic globin gene from a goat DNA recombinant library.";
RL   J. Biol. Chem. 255:6355-6367(1980).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This type of beta-C chain is found when anemia has been
CC       experimentally produced.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; M15389; AAA30914.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; K00662; AAA30921.1; -; Genomic_DNA.
DR   EMBL; K00661; AAA30921.1; JOINED; Genomic_DNA.
DR   PIR; B02396; HBGTC.
DR   RefSeq; XP_005689870.1; XM_005689813.2.
DR   AlphaFoldDB; P02078; -.
DR   SMR; P02078; -.
DR   STRING; 9925.ENSCHIP00000028862; -.
DR   Ensembl; ENSCHIT00000036686; ENSCHIP00000028816; ENSCHIG00000024184.
DR   GeneID; 102175045; -.
DR   KEGG; chx:102175045; -.
DR   CTD; 102175045; -.
DR   GeneTree; ENSGT00940000156216; -.
DR   OMA; SQLHCEK; -.
DR   OrthoDB; 1370439at2759; -.
DR   Proteomes; UP000291000; Chromosome 15.
DR   Bgee; ENSCHIG00000024184; Expressed in metanephros cortex and 16 other tissues.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd08925; Hb-beta-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002337; Hemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   CHAIN           1..142
FT                   /note="Hemoglobin subunit beta-C"
FT                   /id="PRO_0000052910"
FT   BINDING         59
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT   BINDING         88
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
SQ   SEQUENCE   142 AA;  15751 MW;  116CEA369EBD0A33 CRC64;
     MPNKALITGF WSKVKVDEVG AEALGRLLVV YPWTQRFFEH FGDLSSADAV LGNAKVKAHG
     KKVLDSFSNG VQHLDDLKGT FAELSELHCD KLHVDPENFR LLGNVLVIVL ARHFGKEFTP
     ELQAEFQKVV AGVASALAHR YH
 
 
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