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HBBC_OPHSE
ID   HBBC_OPHSE              Reviewed;         146 AA.
AC   B3EWR8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Hemoglobin cathodic subunit beta {ECO:0000303|PubMed:23632627};
DE   AltName: Full=Hemoglobin cathodic beta chain {ECO:0000303|PubMed:23632627};
OS   Ophisurus serpens (Serpent eel) (Muraena serpens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Ophichthidae;
OC   Ophisurus.
OX   NCBI_TaxID=1234705;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:23632627};
RX   PubMed=23632627; DOI=10.1007/s00360-013-0759-y;
RA   Manconi B., Pellegrini M., Messana I., Sanna M.T., Castagnola M.,
RA   Iavarone F., Coluccia E., Giardina B., Olianas A.;
RT   "The hemoglobin system of the serpent eel Ophisurus serpens: structural and
RT   functional characterization.";
RL   J. Comp. Physiol. B 183:905-919(2013).
CC   -!- FUNCTION: Involved in oxygen transport from the gills to various
CC       peripheral tissues. {ECO:0000305|PubMed:23632627}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000250|UniProtKB:P29623}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:23632627}.
CC   -!- MASS SPECTROMETRY: Mass=16004; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23632627};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
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..146
FT                   /note="Hemoglobin cathodic subunit beta"
FT                   /id="PRO_0000423888"
FT   BINDING         63
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                   /evidence="ECO:0000250|UniProtKB:P29623,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   UNSURE          11
FT                   /note="I or L"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          14
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          28
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          31
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          32
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          34
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          48
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          54
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          67
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          68
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          69
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          72
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          84
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          96
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          105
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          106
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          110
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          112
FT                   /note="I or L"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          114
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
FT   UNSURE          141
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:23632627"
SQ   SEQUENCE   146 AA;  15990 MW;  9F0AD6524CBF84EB CRC64;
     VQWSSSERSV ISGLWAKVNA AEVGPQALAR LLVLYPWTQR YFGKFGDLSS NAALMGNANV
     AKHGKDLLLA DLKAVKNMDN VKALYAKXXX XXXXELNVDP DNFTLLGDCL TIVLAMKFGA
     DFTPVDQAVW QKFVAVVVSG LSKQYF
 
 
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