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Q91X72 (HEMO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemopexin
Gene names
Name:Hpx
Synonyms:Hpxn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

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.

Sequence similarities

Belongs to the hemopexin family.

Contains 8 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 460437Hemopexin
PRO_0000021407

Regions

Repeat53 – 9341Hemopexin 1
Repeat94 – 13845Hemopexin 2
Repeat139 – 18345Hemopexin 3
Repeat184 – 23047Hemopexin 4
Repeat257 – 30246Hemopexin 5
Repeat303 – 35048Hemopexin 6
Repeat355 – 39440Hemopexin 7
Repeat398 – 44851Hemopexin 8

Sites

Metal binding791Iron (heme 1 axial ligand) By similarity
Metal binding1491Iron (heme 1 axial ligand) By similarity
Metal binding2351Iron (heme 2 axial ligand) By similarity
Metal binding2911Iron (heme 2 axial ligand) By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Ref.5
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Ref.6
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 230 By similarity
Disulfide bond148 ↔ 153 By similarity
Disulfide bond187 ↔ 199 By similarity
Disulfide bond255 ↔ 458 By similarity
Disulfide bond364 ↔ 406 By similarity
Disulfide bond416 ↔ 433 By similarity

Experimental info

Sequence conflict301N → H in AAH11246. Ref.3
Sequence conflict301N → H in AAH19901. Ref.3
Sequence conflict2331R → Q in AAB49490. Ref.4
Sequence conflict4531Missing in AAB49490. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q91X72 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5DF86BA50CC23B48

FASTA46051,318
        10         20         30         40         50         60 
MARTAVALNI LVLLGLCWSL AVASPLPTAN GRVAEVENGT KPDSDVPEHC LDTWSFDAAT 

        70         80         90        100        110        120 
MDHNGTMLFF KGEFVWRGHS GTRELISARW KNPITSVDAA FRGPDSVFLI KEDKVWVYPP 

       130        140        150        160        170        180 
EKKENGYPKL FQEEFPGIPY PPDAAVECHR GECQSEGVLF FQGNRKWFWD FATRTQKERS 

       190        200        210        220        230        240 
WSTVGNCTAA LRWLERYYCF QGNKFLRFNP VTGEVPPRYP LDARDYFVSC PGRGHGRPRN 

       250        260        270        280        290        300 
GTAHGNSTHP MHSRCSPDPG LTALLSDHRG ATYAFTGSHY WRLDSSRDGW HSWPIAHHWP 

       310        320        330        340        350        360 
QGPSTVDAAF SWDDKVYLIQ GTQVYVFLTK GGNNLVSGYP KRLEKELGSP PGISLETIDA 

       370        380        390        400        410        420 
AFSCPGSSRL YVSSGRRLWW LDLKSGAQAT WTEVSWPHEK VDGALCLDKS LGPNTCSSNG 

       430        440        450        460 
SSLYFIHGPN LYCYSSIDKL NAAKSLPQPQ KVNSILGCSQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]Koepsel R.R., Rohrbach D.H., Brekheiser B.B.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-460.
Tissue: Liver.
[5]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38.
Strain: C57BL/6.
Tissue: Plasma.
[6]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK145928 mRNA. Translation: BAE26759.1.
CH466531 Genomic DNA. Translation: EDL16785.1.
BC011246 mRNA. Translation: AAH11246.1.
BC019901 mRNA. Translation: AAH19901.1.
U89889 mRNA. Translation: AAB49490.1.
RefSeqNP_059067.2. NM_017371.2.
UniGeneMm.3485.

3D structure databases

ProteinModelPortalQ91X72.
SMRQ91X72. Positions 48-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91X72. 4 interactions.
MINTMINT-1862286.

PTM databases

PhosphoSiteQ91X72.

Proteomic databases

PaxDbQ91X72.
PRIDEQ91X72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033185; ENSMUSP00000033185; ENSMUSG00000030895.
GeneID15458.
KEGGmmu:15458.
UCSCuc009iyl.2. mouse.

Organism-specific databases

CTD3263.
MGIMGI:105112. Hpx.

Phylogenomic databases

eggNOGNOG251805.
GeneTreeENSGT00390000009178.
HOGENOMHOG000112887.
HOVERGENHBG005956.
InParanoidQ3UKP2.
OMAAVECHRG.
OrthoDBEOG7Q8CN5.
TreeFamTF331201.

Gene expression databases

BgeeQ91X72.
CleanExMM_HPX.
GenevestigatorQ91X72.

Family and domain databases

Gene3D2.110.10.10. 2 hits.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR016358. Hemopexin_chordata.
IPR018486. Hemopexin_CS.
[Graphical view]
PfamPF00045. Hemopexin. 5 hits.
[Graphical view]
PIRSFPIRSF002551. Hemopexin_chordata. 1 hit.
SMARTSM00120. HX. 6 hits.
[Graphical view]
SUPFAMSSF50923. SSF50923. 2 hits.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHPX. mouse.
NextBio288270.
PROQ91X72.
SOURCESearch...

Entry information

Entry nameHEMO_MOUSE
AccessionPrimary (citable) accession number: Q91X72
Secondary accession number(s): P97824, Q3UKP2, Q8WUP0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot