HEMT_THEHE
ID HEMT_THEHE Reviewed; 113 AA.
AC P02245;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hemerythrin;
OS Themiste hennahi (Peanut worm) (Themiste zostericola).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Themistidae; Themiste.
OX NCBI_TaxID=360549;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=5114534; DOI=10.1021/bi00791a020;
RA Ferrell R.E., Kitto G.B.;
RT "Structural studies on Dendrostomum pyroides hemerythrin.";
RL Biochemistry 10:2923-2929(1971).
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: Homooctamer. {ECO:0000250|UniProtKB:P02244}.
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; A02571; HRTH.
DR AlphaFoldDB; P02245; -.
DR SMR; P02245; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
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..113
FT /note="Hemerythrin"
FT /id="PRO_0000191843"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
SQ SEQUENCE 113 AA; 13421 MW; D44982F4C55654B1 CRC64;
GFPIPDPYGW DPSFRTFYSI IDDEHKTLFN GIFHLAIDDN ADNLGELRRC TGKHFLNQEV
LMQASQYQFY DEHKKAHEEF IRALDNWKGD VKWAKSWLVN HIKTIDFKYK GKI
