Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6ZNA5 (FRRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferric-chelate reductase 1

EC=1.-.-.-
Alternative name(s):
Stromal cell-derived receptor 2
Short name=SDR-2
Gene names
Name:FRRS1
Synonyms:SDFR2, SDR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Ferric-chelate reductases reduce Fe3+ to Fe2+ before its transport from the endosome to the cytoplasm By similarity.

Cofactor

Binds 2 heme groups non-covalently By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the FRRS1 family.

Contains 1 cytochrome b561 domain.

Contains 1 DOMON domain.

Contains 1 reelin domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionferric-chelate reductase activity

Inferred from sequence or structural similarity PubMed 14499595. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZNA5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6ZNA5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     533-592: VHAYRLSRKV...IIFLSAINHL → LKYWMMTEFR...FSLGRLGSCL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Ferric-chelate reductase 1
PRO_0000314843

Regions

Transmembrane2 – 2221Helical; Name=1; Potential
Transmembrane372 – 39221Helical; Name=2; Potential
Transmembrane415 – 43521Helical; Name=3; Potential
Transmembrane446 – 46621Helical; Name=4; Potential
Transmembrane491 – 51121Helical; Name=5; Potential
Transmembrane515 – 53521Helical; Name=6; Potential
Transmembrane569 – 58921Helical; Name=7; Potential
Domain13 – 179167Reelin
Domain216 – 331116DOMON
Domain335 – 534200Cytochrome b561

Sites

Metal binding3731Iron (heme axial ligand) Potential
Metal binding4141Iron (heme axial ligand) Potential
Metal binding4421Iron (heme axial ligand) Potential
Metal binding4711Iron (heme axial ligand) Potential

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence533 – 59260VHAYR…AINHL → LKYWMMTEFRSFSHLLQWKQ RVMLLKRQCWQFMSVGMLLF SSYFYLQSTIYEQAKTLAFA GQVIIIIKPKKLEACPDCLE HICEFSLGRLGSCL in isoform 2.
VSP_030400

Experimental info

Sequence conflict1791P → L in BAD18470. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 21EC19981C4AA95D

FASTA59266,114
        10         20         30         40         50         60 
MAVSGFTLGT CILLLHISYV ANYPNGKVTQ SCHGMIPEHG HSPQSVPVHD IYVSQMTFRP 

        70         80         90        100        110        120 
GDQIEVTLSG HPFKGFLLEA RNAEDLNGPP IGSFTLIDSE VSQLLTCEDI QGSAVSHRSA 

       130        140        150        160        170        180 
SKKTEIKVYW NAPSSAPNHT QFLVTVVEKY KIYWVKIPGP IISQPNAFPF TTPKATVVPL 

       190        200        210        220        230        240 
PTLPPVSHLT KPFSASDCGN KKFCIRSPLN CDPEKEASCV FLSFTRDDQS VMVEMSGPSK 

       250        260        270        280        290        300 
GYLSFALSHD QWMGDDDAYL CIHEDQTVYI QPSHLTGRSH PVMDSRDTLE DMAWRLADGV 

       310        320        330        340        350        360 
MQCSFRRNIT LPGVKNRFDL NTSYYIFLAD GAANDGRIYK HSQQPLITYE KYDVTDSPKN 

       370        380        390        400        410        420 
IGGSHSVLLL KVHGALMFVA WMTTVSIGVL VARFFKPVWS KAFLLGEAAW FQVHRMLMFT 

       430        440        450        460        470        480 
TTVLTCIAFV MPFIYRGGWS RHAGYHPYLG CIVMTLAVLQ PLLAVFRPPL HDPRRQMFNW 

       490        500        510        520        530        540 
THWSMGTAAR IIAVAAMFLG MDLPGLNLPD SWKTYAMTGF VAWHVGTEVV LEVHAYRLSR 

       550        560        570        580        590 
KVEILDDDRI QILQSFTAVE TEGHAFKKAV LAIYVCGNVT FLIIFLSAIN HL 

« Hide

Isoform 2 [UniParc].

Checksum: A8F39D2DFA893E5B
Show »

FASTA62670,465

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Teratocarcinoma.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Cytochrome b561 protein family: expanding roles and versatile transmembrane electron transfer abilities as predicted by a new classification system and protein sequence motif analyses."
Tsubaki M., Takeuchi F., Nakanishi N.
Biochim. Biophys. Acta 1753:174-190(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK131302 mRNA. Translation: BAD18470.1.
AL451051 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW72988.1.
CCDSCCDS30780.1. [Q6ZNA5-2]
RefSeqNP_001013682.2. NM_001013660.2. [Q6ZNA5-2]
XP_005270918.1. XM_005270861.1. [Q6ZNA5-1]
UniGeneHs.454779.

3D structure databases

ProteinModelPortalQ6ZNA5.
SMRQ6ZNA5. Positions 58-154, 368-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000287474.

PTM databases

PhosphoSiteQ6ZNA5.

Polymorphism databases

DMDM166198896.

Proteomic databases

MaxQBQ6ZNA5.
PaxDbQ6ZNA5.
PRIDEQ6ZNA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287474; ENSP00000287474; ENSG00000156869. [Q6ZNA5-2]
ENST00000414213; ENSP00000393884; ENSG00000156869. [Q6ZNA5-1]
GeneID391059.
KEGGhsa:391059.
UCSCuc001dsh.1. human. [Q6ZNA5-2]

Organism-specific databases

CTD391059.
GeneCardsGC01M100174.
HGNCHGNC:27622. FRRS1.
HPAHPA017883.
MIM611578. gene.
neXtProtNX_Q6ZNA5.
PharmGKBPA142670941.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281275.
HOGENOMHOG000112648.
HOVERGENHBG107929.
OMAIPGPIIS.
OrthoDBEOG7K3TKQ.
PhylomeDBQ6ZNA5.
TreeFamTF316169.

Gene expression databases

BgeeQ6ZNA5.
CleanExHS_FRRS1.
GenevestigatorQ6ZNA5.

Family and domain databases

InterProIPR006593. Cyt_b561/ferric_Rdtase_TM.
IPR005018. DOMON_domain.
IPR002861. Reeler_dom.
[Graphical view]
PfamPF03351. DOMON. 1 hit.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTSM00665. B561. 1 hit.
SM00664. DoH. 1 hit.
[Graphical view]
PROSITEPS50939. CYTOCHROME_B561. 1 hit.
PS50836. DOMON. 1 hit.
PS51019. REELIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi391059.
NextBio104295.
PROQ6ZNA5.
SOURCESearch...

Entry information

Entry nameFRRS1_HUMAN
AccessionPrimary (citable) accession number: Q6ZNA5
Secondary accession number(s): A6NLN7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM