Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hemopexin

Gene

HPX

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi151Iron (heme 1 axial ligand)By similarity1
Metal bindingi237Iron (heme 2 axial ligand)By similarity1
Metal bindingi286Iron (heme 2 axial ligand)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemopexin
Alternative name(s):
Hyaluronidase (EC:3.2.1.35)
Gene namesi
Name:HPX
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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 – 281 PublicationAdd BLAST28
ChainiPRO_000002140829 – 459HemopexinAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi52 ↔ 232By similarity
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi150 ↔ 155By similarity
Glycosylationi188N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi189 ↔ 201By similarity
Glycosylationi241N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi250 ↔ 453By similarity
Disulfide bondi359 ↔ 401By similarity
Disulfide bondi411 ↔ 428By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP50828.
PeptideAtlasiP50828.
PRIDEiP50828.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015556.

Structurei

3D structure databases

ProteinModelPortaliP50828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati55 – 95Hemopexin 1Add BLAST41
Repeati96 – 140Hemopexin 2Add BLAST45
Repeati141 – 185Hemopexin 3Add BLAST45
Repeati186 – 232Hemopexin 4Add BLAST47
Repeati252 – 297Hemopexin 5Add BLAST46
Repeati298 – 345Hemopexin 6Add BLAST48
Repeati350 – 389Hemopexin 7Add BLAST40
Repeati393 – 443Hemopexin 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.
InParanoidiP50828.
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. 3 hits.
[Graphical view]
PIRSFiPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTiSM00120. HX. 5 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 2 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARALGTVEA PWLLGLCCSL AIAHPLSLTA GPKHGAEGRN ESKPDPDVTE
60 70 80 90 100
RCSDGWGFDA STLDEHGAML FFKGPSVWAG QNWTRGLISE RWKNAPSSVD
110 120 130 140 150
AAFRRGHDRV FLIQGDKVWV YPPEKEKENP RSLQEEFPGV PSPLDAAVEC
160 170 180 190 200
HRGECQDEGV LFFQGTHTWF WDSTTKTTKE RLWPAVGNCS SAMRWISRYY
210 220 230 240 250
CFRGNQFLRF DPVTGHVDPK YPRDVRDYFM SCPGRGHAHR NATHRGDDRC
260 270 280 290 300
SPDLVLTALL SDNHGATYAF RGTHYWRLDT SRDGWHSWPI DHQWSHGPSA
310 320 330 340 350
VDAAFSWDDK LYLIQGTQVY IFLTKAGYTL VDNYPKQLEK ELGSPHGISL
360 370 380 390 400
DAVDATFVCP GTSRLHVMAG RKLWWLDLSL GAQGPWTELP WPHEKVDAAL
410 420 430 440 450
CTEKSLGPNS CSASGLGLYI VHGPHVYCYK DVEKLVSAKA LPQPQSVNSL

LGCHRSRGS
Length:459
Mass (Da):51,306
Last modified:October 1, 1996 - v1
Checksum:iDB06BB44C29789CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14751 mRNA. Translation: AAC48457.1.
PIRiA55486.
RefSeqiNP_999118.1. NM_213953.2.
UniGeneiSsc.4250.

Genome annotation databases

GeneIDi396998.
KEGGissc:396998.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14751 mRNA. Translation: AAC48457.1.
PIRiA55486.
RefSeqiNP_999118.1. NM_213953.2.
UniGeneiSsc.4250.

3D structure databases

ProteinModelPortaliP50828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015556.

Proteomic databases

PaxDbiP50828.
PeptideAtlasiP50828.
PRIDEiP50828.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396998.
KEGGissc:396998.

Organism-specific databases

CTDi3263.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000112887.
HOVERGENiHBG005956.
InParanoidiP50828.
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. 3 hits.
[Graphical view]
PIRSFiPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTiSM00120. HX. 5 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 2 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEMO_PIG
AccessioniPrimary (citable) accession number: P50828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 101 of the entry and version 1 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 (By similarity).By similarity

Caution

Lacks the conserved His heme iron ligand in position 81. There is a Gln in this position.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.