ID   GLB3_TYLHE              Reviewed;         148 AA.
AC   P13578;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Extracellular globin-2B;
DE   AltName: Full=Erythrocruorin;
DE   AltName: Full=Extracellular globin IIB;
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=4044566; DOI=10.1016/s0021-9258(17)39054-3;
RA   Suzuki T., Yasunaga H., Furukohri T., Nakamura K., Gotoh T.;
RT   "Amino acid sequence of polypeptide chain IIB of extracellular hemoglobin
RT   from the polychaete Tylorrhynchus heterochaetus.";
RL   J. Biol. Chem. 260:11481-11487(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: Disulfide bonded trimer of chains IIA, IIB, and IIC.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Giant hemoglobins of worms are formed of a monomeric
CC       subunit and a disulfide-bonded trimer.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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   AlphaFoldDB; P13578; -.
DR   SMR; P13578; -.
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..148
FT                   /note="Extracellular globin-2B"
FT                   /id="PRO_0000052514"
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 IID)"
FT                   /evidence="ECO:0000269|PubMed:3192547"
FT   DISULFID        4..135
FT                   /evidence="ECO:0000269|PubMed:3192547"
SQ   SEQUENCE   148 AA;  16680 MW;  40DD2369EAD054D8 CRC64;
     DDCCSAADRH EVLDNWKGIW SAEFTGRRVA IGQAIFQELF ALDPNAKGVF GRVNVDKPSE
     ADWKAHVIRV INGLDLAVNL LEDPKALQEE LKHLARQHRE RSGVKAVYFD EMEKALLKVL
     PQVSSHFNSG AWDRCFTRIA DVIKAELP