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 13-SEP-2023, entry version 84. DE RecName: Full=Hemerythrin; OS Siphonosoma cumanense (Sipunculan worm) (Lumbricus edulis). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Sipuncula; OC Sipunculidea; 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}. 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; 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; Hemerythrin-like; 1. DR InterPro; IPR002063; Haemerythrin. DR InterPro; IPR016131; Haemerythrin_Fe_BS. DR InterPro; IPR035938; Hemerythrin-like_sf. DR InterPro; IPR012827; Hemerythrin_metal-bd. DR NCBIfam; TIGR00058; Hemerythrin; 1. DR PANTHER; PTHR37164; BACTERIOHEMERYTHRIN; 1. DR PANTHER; PTHR37164:SF1; BACTERIOHEMERYTHRIN; 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 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 //