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Protein

Hemopexin

Gene

HPX

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Iron (heme 1 axial ligand)
Metal bindingi152 – 1521Iron (heme 1 axial ligand)
Metal bindingi238 – 2381Iron (heme 2 axial ligand)
Metal bindingi291 – 2911Iron (heme 2 axial ligand)

GO - Molecular functioni

  • heme binding Source: MGI
  • heme transporter activity Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemopexin
Gene namesi
Name:HPX
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 460435HemopexinPRO_0000021409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)
Disulfide bondi52 ↔ 233
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi151 ↔ 156
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi190 ↔ 202
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi255 ↔ 458
Disulfide bondi364 ↔ 406
Disulfide bondi416 ↔ 433

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021163.

Structurei

Secondary structure

1
460
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 523Combined sources
Beta strandi59 – 635Combined sources
Beta strandi69 – 735Combined sources
Beta strandi76 – 794Combined sources
Turni80 – 834Combined sources
Beta strandi84 – 874Combined sources
Helixi88 – 914Combined sources
Beta strandi100 – 1056Combined sources
Turni106 – 1083Combined sources
Beta strandi109 – 1146Combined sources
Beta strandi117 – 1215Combined sources
Helixi134 – 1374Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi156 – 16510Combined sources
Beta strandi168 – 1736Combined sources
Turni174 – 1774Combined sources
Beta strandi178 – 1825Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi207 – 2115Combined sources
Turni213 – 2153Combined sources
Helixi226 – 2294Combined sources
Helixi253 – 2553Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi279 – 2879Combined sources
Beta strandi292 – 2943Combined sources
Helixi295 – 2973Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi323 – 3286Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi340 – 3423Combined sources
Helixi343 – 3475Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi369 – 3746Combined sources
Beta strandi377 – 3826Combined sources
Helixi383 – 3886Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi422 – 4276Combined sources
Beta strandi430 – 4367Combined sources
Helixi437 – 4426Combined sources
Helixi452 – 4554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXNX-ray1.80A242-460[»]
1QHUX-ray2.30A1-460[»]
1QJSX-ray2.90A/B1-460[»]
ProteinModelPortaliP20058.
SMRiP20058. Positions 49-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20058.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati55 – 9541Hemopexin 1Add
BLAST
Repeati96 – 14146Hemopexin 2Add
BLAST
Repeati142 – 18645Hemopexin 3Add
BLAST
Repeati187 – 23347Hemopexin 4Add
BLAST
Repeati257 – 30246Hemopexin 5Add
BLAST
Repeati303 – 35048Hemopexin 6Add
BLAST
Repeati355 – 39440Hemopexin 7Add
BLAST
Repeati398 – 44851Hemopexin 8Add
BLAST

Sequence similaritiesi

Belongs to the hemopexin family.Curated
Contains 8 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000112887.
HOVERGENiHBG005956.
InParanoidiP20058.
KOiK18977.

Family and domain databases

Gene3Di2.110.10.10. 2 hits.
InterProiIPR016358. Hemopexin.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
[Graphical view]
PIRSFiPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTiSM00120. HX. 5 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 2 hits.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKASGIPIA LGVWGLCWSL ATVNSVPLTS AHGNVTEGES GTKPEADVIE
60 70 80 90 100
QCSDGWSFDA TTLDDNGTML FFKDEFVWKS HRGIRELISE RWKNFIGPVD
110 120 130 140 150
AAFRHGHTSV YLIKGDKVWV YTSEKNEKVY PKSLQDEFPG IPFPLDAAVE
160 170 180 190 200
CHRGECQDEG ILFFQGNRKW FWDLTTGTKK ERSWPAVGNC TSALRWLGRY
210 220 230 240 250
YCFQGNQFLR FNPVSGEVPP GYPLDVRDYF LSCPGRGHRS SHRNSTQHGH
260 270 280 290 300
ESTRCDPDLV LSAMVSDNHG ATYVFSGSHY WRLDTNRDGW HSWPIAHQWP
310 320 330 340 350
QGPSTVDAAF SWEDKLYLIQ DTKVYVFLTK GGYTLVNGYP KRLEKELGSP
360 370 380 390 400
PVISLEAVDA AFVCPGSSRL HIMAGRRLWW LDLKSGAQAT WTELPWPHEK
410 420 430 440 450
VDGALCMEKP LGPNSCSTSG PNLYLIHGPN LYCYRHVDKL NAAKNLPQPQ
460
RVSRLLGCTH
Length:460
Mass (Da):51,767
Last modified:October 1, 1996 - v2
Checksum:i193B59856DEF64EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521C → W AA sequence (PubMed:3421961).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16429 mRNA. Translation: CAA34452.1.
PIRiA46006. OQRB.
RefSeqiNP_001076229.1. NM_001082760.1.
UniGeneiOcu.3101.

Genome annotation databases

GeneIDi100009541.
KEGGiocu:100009541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16429 mRNA. Translation: CAA34452.1.
PIRiA46006. OQRB.
RefSeqiNP_001076229.1. NM_001082760.1.
UniGeneiOcu.3101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXNX-ray1.80A242-460[»]
1QHUX-ray2.30A1-460[»]
1QJSX-ray2.90A/B1-460[»]
ProteinModelPortaliP20058.
SMRiP20058. Positions 49-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009541.
KEGGiocu:100009541.

Organism-specific databases

CTDi3263.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000112887.
HOVERGENiHBG005956.
InParanoidiP20058.
KOiK18977.

Miscellaneous databases

EvolutionaryTraceiP20058.

Family and domain databases

Gene3Di2.110.10.10. 2 hits.
InterProiIPR016358. Hemopexin.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
[Graphical view]
PIRSFiPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTiSM00120. HX. 5 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 2 hits.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region."
    Morgan W.T., Muster P., Tatum F., Kao S.-M., Alam J., Smith A.
    J. Biol. Chem. 268:6256-6262(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, HEME-BINDING SITES.
    Tissue: Liver.
  2. "N-terminal amino acid sequences of the hemopexins from chicken, rat and rabbit."
    Wellner D., Cheng K.C., Mueller-Eberhard U.
    Biochem. Biophys. Res. Commun. 155:622-625(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-53.
  3. "1.8-A crystal structure of the C-terminal domain of rabbit serum haemopexin."
    Faber H.R., Groom C.R., Baker H.M., Morgan W.T., Smith A., Baker E.N.
    Structure 3:551-559(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 242-460, DISULFIDE BONDS.
  4. "Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains."
    Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., Baker E.N.
    Nat. Struct. Biol. 6:926-931(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME, DISULFIDE BONDS.

Entry informationi

Entry nameiHEMO_RABIT
AccessioniPrimary (citable) accession number: P20058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: December 9, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The isolated N-terminal domain binds one heme. The full-length protein also binds one heme, but at a different site. The physiological significance of this is not clear.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.