HEMTA_LINUN
ID HEMTA_LINUN Reviewed; 117 AA.
AC P22764;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Hemerythrin subunit alpha;
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1769966; DOI=10.1093/oxfordjournals.jbchem.a123589;
RA Yano H., Satake K., Ueno Y., Kondo K., Tsugita A.;
RT "Amino acid sequence of the hemerythrin alpha subunit from Lingula
RT unguis.";
RL J. Biochem. 110:376-380(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-41 AND 110-117.
RX PubMed=2315298;
RA Satake K., Yugi M., Kamo M., Kihara H., Tsugita A.;
RT "Hemerythrin from Lingula unguis consists of two different subunits, alpha
RT and beta.";
RL Protein Seq. Data Anal. 3:1-5(1990).
CC -!- FUNCTION: Hemerythrin is a respiratory protein in blood cells of
CC certain marine worms. The oxygen-binding site in each chain contains
CC two iron atoms.
CC -!- SUBUNIT: Octamer composed of two types of chains: alpha and beta.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; JX0184; JX0184.
DR AlphaFoldDB; P22764; -.
DR SMR; P22764; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProt.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR Pfam; PF01814; Hemerythrin; 1.
DR PIRSF; PIRSF002033; Hemerythrin; 1.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR TIGRFAMs; TIGR00058; Hemerythrin; 1.
DR PROSITE; PS00550; HEMERYTHRINS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..117
FT /note="Hemerythrin subunit alpha"
FT /id="PRO_0000191830"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 53
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 72
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT CONFLICT 112
FT /note="K -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 117 AA; 13905 MW; 5EB2F77B2D4BABCB CRC64;
VKVPEPFAWN ESFATSYKNI DLEHRTLFNG LFALSEFNTR DQLLACKEVF VMHFRDEQGQ
MEKANYEHFE EHRGIHEGFL EKMGHWKAPV AQKDIKFGME WLVNHIPTED FKYKGKL
