HEMT_SIPCU
ID HEMT_SIPCU Reviewed; 113 AA.
AC P22766;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Hemerythrin;
OS Siphonosoma cumanense (Sipunculan worm) (Lumbricus edulis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Sipunculidae; Siphonosoma.
OX NCBI_TaxID=6444;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2362933;
RA Uchida T., Yano H., Satake K., Kubota I., Tsugita A.;
RT "The amino acid sequence of hemerythrin from Siphonosoma cumanense.";
RL Protein Seq. Data Anal. 3:141-147(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: Homotrimer.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; JT0556; HRIN.
DR AlphaFoldDB; P22766; -.
DR SMR; P22766; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd12107; Hemerythrin; 1.
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; 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_0000191838"
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"
FT VARIANT 3
FT /note="P -> E"
FT VARIANT 10
FT /note="W -> D"
FT VARIANT 60
FT /note="A -> G"
FT VARIANT 66
FT /note="K -> N"
FT VARIANT 83
FT /note="K -> Q"
SQ SEQUENCE 113 AA; 12437 MW; 653C278D78F9E953 CRC64;
GFPVPDPFIW DASFKTFYDD LDNQHKQLFQ AILTQGNVGG ATAGDNAYAC LVAHFLFEEA
AMQVAKYGGY GAHKAAHEEF LGKVKGGSAD AAYCKDWLTQ HIKTIDFKYK GKL