HEMTA_LINRE
ID HEMTA_LINRE Reviewed; 117 AA.
AC P23543; Q7M412;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Hemerythrin subunit alpha;
OS Lingula reevii (Inarticulated brachiopod).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7575;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7947959; DOI=10.1016/0167-4838(94)90114-7;
RA Negri A., Tedeschi G., Bonomi F., Zhang J.-H., Kurtz D.M. Jr.;
RT "Amino-acid sequences of the alpha- and beta-subunits of hemerythrin from
RT Lingula reevii.";
RL Biochim. Biophys. Acta 1208:277-285(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-24.
RX PubMed=1892823; DOI=10.1021/bi00102a001;
RA Zhang J.-H., Kurtz D.M. Jr.;
RT "Two distinct subunits of hemerythrin from the brachiopod Lingula reevii:
RT an apparent requirement for cooperativity in O2 binding.";
RL Biochemistry 30:9121-9124(1991).
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; S50177; S50177.
DR AlphaFoldDB; P23543; -.
DR SMR; P23543; -.
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 Transport.
FT CHAIN 1..117
FT /note="Hemerythrin subunit alpha"
FT /id="PRO_0000191828"
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"
SQ SEQUENCE 117 AA; 13878 MW; BF553CDD71F2019B CRC64;
VKVPAPFAWN EDFATSYKFI DLEHRTLFNG LFALSEFNTR DQLLACKEVF VMHFRDEQGQ
MEKANYEHFE EHKGIHEGFL EKMGHWKAPV AQKDIRFGME WLVNHIPAED FKYKGKL
