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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)DescriptionActionsGraphical viewLength
Metal bindingi81Iron (heme 1 axial ligand)1
Metal bindingi152Iron (heme 1 axial ligand)1
Metal bindingi238Iron (heme 2 axial ligand)1
Metal bindingi291Iron (heme 2 axial ligand)1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000002140926 – 460HemopexinAdd BLAST435

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...)1
Disulfide bondi52 ↔ 233
Glycosylationi66N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi151 ↔ 156
Glycosylationi189N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi190 ↔ 202
Glycosylationi244N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi255 ↔ 458
Disulfide bondi364 ↔ 406
Disulfide bondi416 ↔ 433

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP20058.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021163.

Structurei

Secondary structure

1460
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 52Combined sources3
Beta strandi59 – 63Combined sources5
Beta strandi69 – 73Combined sources5
Beta strandi76 – 79Combined sources4
Turni80 – 83Combined sources4
Beta strandi84 – 87Combined sources4
Helixi88 – 91Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi100 – 105Combined sources6
Turni106 – 108Combined sources3
Beta strandi109 – 114Combined sources6
Beta strandi117 – 121Combined sources5
Helixi134 – 137Combined sources4
Beta strandi147 – 151Combined sources5
Beta strandi156 – 165Combined sources10
Beta strandi168 – 173Combined sources6
Turni174 – 177Combined sources4
Beta strandi178 – 182Combined sources5
Beta strandi185 – 187Combined sources3
Beta strandi191 – 196Combined sources6
Beta strandi199 – 204Combined sources6
Beta strandi207 – 211Combined sources5
Turni213 – 215Combined sources3
Helixi226 – 229Combined sources4
Helixi253 – 255Combined sources3
Beta strandi263 – 266Combined sources4
Beta strandi272 – 276Combined sources5
Beta strandi279 – 287Combined sources9
Beta strandi292 – 294Combined sources3
Helixi295 – 297Combined sources3
Beta strandi307 – 312Combined sources6
Beta strandi315 – 320Combined sources6
Beta strandi323 – 328Combined sources6
Beta strandi330 – 332Combined sources3
Beta strandi340 – 342Combined sources3
Helixi343 – 347Combined sources5
Beta strandi360 – 362Combined sources3
Beta strandi369 – 374Combined sources6
Beta strandi377 – 382Combined sources6
Helixi383 – 388Combined sources6
Beta strandi392 – 394Combined sources3
Beta strandi402 – 409Combined sources8
Beta strandi411 – 413Combined sources3
Beta strandi418 – 420Combined sources3
Beta strandi422 – 427Combined sources6
Beta strandi430 – 436Combined sources7
Helixi437 – 442Combined sources6
Helixi452 – 455Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HXNX-ray1.80A242-460[»]
1QHUX-ray2.30A1-460[»]
1QJSX-ray2.90A/B1-460[»]
4RT6X-ray2.80B26-239[»]
ProteinModelPortaliP20058.
SMRiP20058.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20058.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati55 – 95Hemopexin 1Add BLAST41
Repeati96 – 141Hemopexin 2Add BLAST46
Repeati142 – 186Hemopexin 3Add BLAST45
Repeati187 – 233Hemopexin 4Add BLAST47
Repeati257 – 302Hemopexin 5Add BLAST46
Repeati303 – 350Hemopexin 6Add BLAST48
Repeati355 – 394Hemopexin 7Add BLAST40
Repeati398 – 448Hemopexin 8Add BLAST51

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

CDDicd00094. HX. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti52C → W AA sequence (PubMed:3421961).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HXNX-ray1.80A242-460[»]
1QHUX-ray2.30A1-460[»]
1QJSX-ray2.90A/B1-460[»]
4RT6X-ray2.80B26-239[»]
ProteinModelPortaliP20058.
SMRiP20058.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000021163.

Proteomic databases

PRIDEiP20058.

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

CDDicd00094. HX. 2 hits.
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...

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: November 30, 2016
This is version 118 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.