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HBBN_AMMLE
ID   HBBN_AMMLE              Reviewed;         141 AA.
AC   P02080;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Hemoglobin subunit beta-C(NA);
DE   AltName: Full=Beta-C(NA)-globin;
DE   AltName: Full=Hemoglobin beta C(NA) chain;
OS   Ammotragus lervia (Barbary sheep) (Antilope lervia).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ammotragus.
OX   NCBI_TaxID=9899;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE.
RX   PubMed=16742600; DOI=10.1042/bj1070745;
RA   Huisman T.H.J., Dasher G.A., Moretz W.H. Jr., Dozy A.M., Wilson J.B.,
RA   van Vliet G.;
RT   "Studies of haemoglobin types in Barbary sheep (Ammotragus lervia).";
RL   Biochem. J. 107:745-751(1968).
RN   [2]
RP   SEQUENCE REVISION TO 103.
RA   Huisman T.H.J.;
RL   Submitted (JAN-1969) to the PIR data bank.
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 in non-anemic barbary
CC       sheep, whereas the other type of beta C chain is found in anemic
CC       barbary sheep.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A90239; HBSHBC.
DR   PRIDE; P02080; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit beta-C(NA)"
FT                   /id="PRO_0000052865"
FT   BINDING         58
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         87
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   141 AA;  15635 MW;  394652AA5100FA33 CRC64;
     PBKALITGFW SKVKVBZVGA ZALGRLLVVY PWTZRFFZHF GBLSSABAVM BBAKVKAHGK
     KVLBSFSBGL KHLBBLKGAF ASLSZLHCBK LHVBPZBFRL LGBVLVVVLA RHFGKZFBPZ
     LZAZFZKVVA GVASALAHRY H
 
 
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