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GLB2_TYLHE
ID   GLB2_TYLHE              Reviewed;         146 AA.
AC   P09966;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Extracellular globin-2A;
DE   AltName: Full=Erythrocruorin;
DE   AltName: Full=Globin IIA;
OS   Tylorrhynchus heterochaetus (Marine worm) (Nereis heterochaeta).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Tylorrhynchus.
OX   NCBI_TaxID=6361;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3722198; DOI=10.1016/s0021-9258(18)67648-3;
RA   Suzuki T., Gotoh T.;
RT   "The complete amino acid sequence of giant multisubunit hemoglobin from the
RT   polychaete Tylorrhynchus heterochaetus.";
RL   J. Biol. Chem. 261:9257-9267(1986).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=3192547; DOI=10.1016/s0021-9258(19)81390-x;
RA   Suzuki T., Kapp O.H., Gotoh T.;
RT   "Novel S-S loops in the giant hemoglobin of Tylorrhynchus heterochaetus.";
RL   J. Biol. Chem. 263:18524-18529(1988).
CC   -!- SUBUNIT: Disulfide bonded trimer of chains IIA, IIB, and IIC.
CC   -!- MISCELLANEOUS: Giant hemoglobins of worms are formed of a monomeric
CC       subunit and a disulfide-bonded trimer.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A24811; A24811.
DR   AlphaFoldDB; P09966; -.
DR   SMR; P09966; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR002336; Erythrocruorin.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR014610; Haemoglobin_extracell.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PIRSF; PIRSF036517; Ext_hemo; 1.
DR   PRINTS; PR00611; ERYTHCRUORIN.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..146
FT                   /note="Extracellular globin-2A"
FT                   /id="PRO_0000052513"
FT   BINDING         97
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"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   DISULFID        5..134
FT                   /evidence="ECO:0000269|PubMed:3192547"
FT   DISULFID        125
FT                   /note="Interchain (with chain IIC)"
FT                   /evidence="ECO:0000269|PubMed:3192547"
SQ   SEQUENCE   146 AA;  16602 MW;  67E74FB39BD351E9 CRC64;
     SSDHCGPLQR LKVKQQWAKA YGVGHERVEL GIALWKSMFA QDNDARDLFK RVHGEDVHSP
     AFEAHMARVF NGLDRVISSL TDEPVLNAQL EHLRQQHIKL GITGHMFNLM RTGLAYVLPA
     QLGRCFDKEA WAACWDEVIY PGIKHD
 
 
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