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HEMO_PONAB
ID   HEMO_PONAB              Reviewed;         462 AA.
AC   Q5R543; Q5NVR6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Hemopexin;
DE   Flags: Precursor;
GN   Name=HPX;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds heme and transports it to the liver for breakdown and
CC       iron recovery, after which the free hemopexin returns to the
CC       circulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- MISCELLANEOUS: The isolated N-terminal domain binds one heme. The full-
CC       length protein also binds one heme, but at a different site. The
CC       physiological significance of this is not clear (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
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DR   EMBL; CR861031; CAH93123.1; -; mRNA.
DR   EMBL; CR925939; CAI29597.1; -; mRNA.
DR   RefSeq; NP_001127067.1; NM_001133595.1.
DR   AlphaFoldDB; Q5R543; -.
DR   SMR; Q5R543; -.
DR   STRING; 9601.ENSPPYP00000004063; -.
DR   PRIDE; Q5R543; -.
DR   Ensembl; ENSPPYT00000004222; ENSPPYP00000004063; ENSPPYG00000003544.
DR   GeneID; 100174097; -.
DR   KEGG; pon:100174097; -.
DR   CTD; 3263; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00390000009178; -.
DR   HOGENOM; CLU_061713_0_0_1; -.
DR   InParanoid; Q5R543; -.
DR   OMA; CSSAMRW; -.
DR   OrthoDB; 792317at2759; -.
DR   TreeFam; TF331201; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0015232; F:heme transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0042168; P:heme metabolic process; IEA:Ensembl.
DR   GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR   GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   CDD; cd00094; HX; 2.
DR   Gene3D; 2.110.10.10; -; 2.
DR   InterPro; IPR016358; Hemopexin.
DR   InterPro; IPR000585; Hemopexin-like_dom.
DR   InterPro; IPR036375; Hemopexin-like_dom_sf.
DR   InterPro; IPR018487; Hemopexin-like_repeat.
DR   InterPro; IPR018486; Hemopexin_CS.
DR   Pfam; PF00045; Hemopexin; 5.
DR   PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR   SMART; SM00120; HX; 5.
DR   SUPFAM; SSF50923; SSF50923; 2.
DR   PROSITE; PS00024; HEMOPEXIN; 2.
DR   PROSITE; PS51642; HEMOPEXIN_2; 8.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..462
FT                   /note="Hemopexin"
FT                   /id="PRO_0000353185"
FT   REPEAT          53..93
FT                   /note="Hemopexin 1"
FT   REPEAT          94..139
FT                   /note="Hemopexin 2"
FT   REPEAT          140..184
FT                   /note="Hemopexin 3"
FT   REPEAT          185..231
FT                   /note="Hemopexin 4"
FT   REPEAT          259..304
FT                   /note="Hemopexin 5"
FT   REPEAT          305..352
FT                   /note="Hemopexin 6"
FT   REPEAT          357..396
FT                   /note="Hemopexin 7"
FT   REPEAT          400..450
FT                   /note="Hemopexin 8"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..231
FT                   /evidence="ECO:0000250"
FT   DISULFID        149..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        188..200
FT                   /evidence="ECO:0000250"
FT   DISULFID        257..460
FT                   /evidence="ECO:0000250"
FT   DISULFID        366..408
FT                   /evidence="ECO:0000250"
FT   DISULFID        418..435
FT                   /evidence="ECO:0000250"
FT   CONFLICT        390
FT                   /note="Q -> K (in Ref. 1; CAI29597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  51614 MW;  E7EDB4CC1668AC4D CRC64;
     MARALGAPIA LGLWSLCWSL AIATPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT
     LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP
     PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER
     SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN
     GTGHGNGTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ
     WPQGPSTVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKQLEKEVG TPHGIILDSV
     DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ALWTELPWPH EKVDGALCVE KSLGPNSCSA
     NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH
 
 
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