ID   HEMTA_LINAN             Reviewed;         117 AA.
AC   P22764;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 3.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Hemerythrin subunit alpha;
OS   Lingula anatina (Brachiopod) (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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; JX0184; JX0184.
DR   AlphaFoldDB; P22764; -.
DR   SMR; P22764; -.
DR   InParanoid; P22764; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   CDD; cd12107; Hemerythrin; 1.
DR   Gene3D; 1.20.120.50; Hemerythrin-like; 1.
DR   InterPro; IPR002063; Haemerythrin.
DR   InterPro; IPR016131; Haemerythrin_Fe_BS.
DR   InterPro; IPR050669; Hemerythrin.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR035938; Hemerythrin-like_sf.
DR   InterPro; IPR012827; Hemerythrin_metal-bd.
DR   NCBIfam; TIGR02481; hemeryth_dom; 1.
DR   NCBIfam; TIGR00058; Hemerythrin; 1.
DR   PANTHER; PTHR37164; BACTERIOHEMERYTHRIN; 1.
DR   PANTHER; PTHR37164:SF1; BACTERIOHEMERYTHRIN; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
DR   PIRSF; PIRSF002033; Hemerythrin; 1.
DR   PRINTS; PR00186; HEMERYTHRIN.
DR   SUPFAM; SSF47188; Hemerythrin-like; 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
//