ID   HBL0_PHYPA              Reviewed;         180 AA.
AC   Q9M630; A0FKM9; A9SEU7; E1C9X3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Non-symbiotic hemoglobin 0;
DE   AltName: Full=Non-vascular plant hemoglobin Glb0;
GN   Name=GLB0; ORFNames=PHYPADRAFT_184189;
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Arredondo-Peter R., Ramirez M., Sarath G., Klucas R.V.;
RT   "Sequence analysis of an ancient hemoglobin cDNA isolated from the moss
RT   Physcomitrella patens.";
RL   (er) Plant Gene Register PGR00-040(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11725952; DOI=10.1023/a:1012440926982;
RA   Hunt P.W., Watts R.A., Trevaskis B., Llewellyn D.J., Burnell J.,
RA   Dennis E.S., Peacock W.J.;
RT   "Expression and evolution of functionally distinct haemoglobin genes in
RT   plants.";
RL   Plant Mol. Biol. 47:677-692(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Gametophyte;
RA   Garrocho-Villegas V., Arredondo-Peter R.;
RT   "Cloning of Physcomitrella patens non-symbiotic hemoglobin gene.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
CC   -!- FUNCTION: May not function as an oxygen storage or transport protein,
CC       but might act as an oxygen sensor. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the plant globin family. {ECO:0000305}.
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DR   EMBL; AF218049; AAF66104.1; -; mRNA.
DR   EMBL; AY026342; AAK14807.1; -; mRNA.
DR   EMBL; EF028055; ABK20873.1; -; Genomic_DNA.
DR   EMBL; DS544960; EDQ70344.1; -; Genomic_DNA.
DR   RefSeq; XP_001764902.1; XM_001764850.1.
DR   AlphaFoldDB; Q9M630; -.
DR   SMR; Q9M630; -.
DR   STRING; 3218.PP1S71_207V6.1; -.
DR   EnsemblPlants; Pp3c22_15040V3.1; Pp3c22_15040V3.1; Pp3c22_15040.
DR   EnsemblPlants; Pp3c22_15040V3.2; Pp3c22_15040V3.2; Pp3c22_15040.
DR   EnsemblPlants; Pp3c22_15040V3.3; Pp3c22_15040V3.3; Pp3c22_15040.
DR   EnsemblPlants; Pp3c22_15040V3.5; Pp3c22_15040V3.5; Pp3c22_15040.
DR   Gramene; Pp3c22_15040V3.1; Pp3c22_15040V3.1; Pp3c22_15040.
DR   Gramene; Pp3c22_15040V3.2; Pp3c22_15040V3.2; Pp3c22_15040.
DR   Gramene; Pp3c22_15040V3.3; Pp3c22_15040V3.3; Pp3c22_15040.
DR   Gramene; Pp3c22_15040V3.5; Pp3c22_15040V3.5; Pp3c22_15040.
DR   eggNOG; KOG3378; Eukaryota.
DR   HOGENOM; CLU_003827_11_2_1; -.
DR   InParanoid; Q9M630; -.
DR   OMA; MRQGYQD; -.
DR   OrthoDB; 1379813at2759; -.
DR   Proteomes; UP000006727; Chromosome 22.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR001032; Leghaemoglobin.
DR   InterPro; IPR019824; Leghaemoglobin_Fe_BS.
DR   PANTHER; PTHR22924; PTHR22924; 1.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS00208; PLANT_GLOBIN; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   CHAIN           1..180
FT                   /note="Non-symbiotic hemoglobin 0"
FT                   /id="PRO_0000193025"
FT   BINDING         84
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         119
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"
SQ   SEQUENCE   180 AA;  20001 MW;  489374A94E9767BE CRC64;
     MASAVVNQSE AAAVRAPSKP VKTYSKENEQ LVKQSWEILK KDAQRNGINF FRKVFEIAPG
     AKAMYSFLRD STIPFEENPK VKNHARYVFM MTGDAAVQLG EKGAYQVLES KLQKLAATHV
     NAGVTDDQFE IVKEAILYAI EMGVPDLWSP ELKSAWGDAY DMLAEQVKAE MHAQRSAATS