ID   GLB4_TYLHE              Reviewed;         149 AA.
AC   P02220;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Extracellular globin-2C;
DE   AltName: Full=Erythrocruorin;
DE   AltName: Full=Extracellular globin IIC;
OS   Tylorrhynchus heterochaetus (Marine worm) (Nereis heterochaeta).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Nereididae; Tylorrhynchus.
OX   NCBI_TaxID=6361;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3972820; DOI=10.1016/s0021-9258(18)89485-6;
RA   Suzuki T., Furukohri T., Gotoh T.;
RT   "Subunit structure of extracellular hemoglobin from the polychaete
RT   Tylorrhynchus heterochaetus and amino acid sequence of the constituent
RT   polypeptide chain (IIC).";
RL   J. Biol. Chem. 260:3145-3154(1985).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=3192547; DOI=10.1016/s0021-9258(19)81390-x;
RA   Suzuki T., Kapp O.H., Gotoh T.;
RT   "Novel S-S loops in the giant hemoglobin of Tylorrhynchus heterochaetus.";
RL   J. Biol. Chem. 263:18524-18529(1988).
CC   -!- SUBUNIT: Giant hemoglobins of worms are formed of a monomeric subunit
CC       and a disulfide-bonded trimer. IIC is part of the disulfide bonded
CC       trimer composed of IIA, IIB and IIC.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A02542; GGWN2C.
DR   AlphaFoldDB; P02220; -.
DR   SMR; P02220; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR014610; Haemoglobin_extracell.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PIRSF; PIRSF036517; Ext_hemo; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Heme; Iron; Metal-binding;
KW   Oxygen transport; Secreted; Transport.
FT   CHAIN           1..149
FT                   /note="Extracellular globin-2C"
FT                   /id="PRO_0000052516"
FT   BINDING         98
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   DISULFID        3
FT                   /note="Interchain (with chain IIB)"
FT                   /evidence="ECO:0000269|PubMed:3192547"
FT   DISULFID        4..126
FT                   /evidence="ECO:0000269|PubMed:3192547"
FT   DISULFID        135
FT                   /note="Interchain (with chain IIA)"
FT                   /evidence="ECO:0000269|PubMed:3192547"
SQ   SEQUENCE   149 AA;  16795 MW;  6567417159F70C4D CRC64;
     DTCCSIEDRR EVQALWRSIW SAEDTGRRTL IGRLLFEELF EIDGATKGLF KRVNVDDTHS
     PEEFAHVLRV VNGLDTLIGV LGDSDTLNSL IDHLAEQHKA RAGFKTVYFK EFGKALNHVL
     PEVASCFNPE AWNHCFDGLV DVISHRIDG