Q6ZNA5 (FRRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Electron transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ferric-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	Ferric-chelate reductase 1		PRO_0000314843
Regions
	Transmembrane	2 – 22	21	Helical; Name=1; Potential
	Transmembrane	372 – 392	21	Helical; Name=2; Potential
	Transmembrane	415 – 435	21	Helical; Name=3; Potential
	Transmembrane	446 – 466	21	Helical; Name=4; Potential
	Transmembrane	491 – 511	21	Helical; Name=5; Potential
	Transmembrane	515 – 535	21	Helical; Name=6; Potential
	Transmembrane	569 – 589	21	Helical; Name=7; Potential
	Domain	13 – 179	167	Reelin
	Domain	216 – 331	116	DOMON
	Domain	335 – 534	200	Cytochrome b561
Sites
	Metal binding	373	1	Iron (heme axial ligand) Potential
	Metal binding	414	1	Iron (heme axial ligand) Potential
	Metal binding	442	1	Iron (heme axial ligand) Potential
	Metal binding	471	1	Iron (heme axial ligand) Potential
Amino acid modifications
	Glycosylation	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	308	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	533 – 592	60	VHAYR…AINHL → LKYWMMTEFRSFSHLLQWKQ RVMLLKRQCWQFMSVGMLLF SSYFYLQSTIYEQAKTLAFA GQVIIIIKPKKLEACPDCLE HICEFSLGRLGSCL in isoform 2.		VSP_030400
Experimental info
	Sequence conflict	179	1	P → L in BAD18470. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 21EC19981C4AA95D	FASTA	592	66,114
	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
	Isoform 2 [UniParc]. Checksum: A8F39D2DFA893E5B	FASTA	626	70,465
	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 LELKYWMMTE 550 560 570 580 590 600 FRSFSHLLQW KQRVMLLKRQ CWQFMSVGML LFSSYFYLQS TIYEQAKTLA FAGQVIIIIK 610 620 PKKLEACPDC LEHICEFSLG RLGSCL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00418594. IPI00878384.
RefSeq	NP_001013682.2. NM_001013660.2.
UniGene	Hs.454779.
3D structure databases
ProteinModelPortal	Q6ZNA5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000287474.
PTM databases
PhosphoSite	Q6ZNA5.
Polymorphism databases
DMDM	166198896.
Proteomic databases
PaxDb	Q6ZNA5.
PRIDE	Q6ZNA5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000287474; ENSP00000287474; ENSG00000156869. ENST00000414213; ENSP00000393884; ENSG00000156869.
GeneID	391059.
KEGG	hsa:391059.
UCSC	uc001dsh.1. human.
Organism-specific databases
CTD	391059.
GeneCards	GC01M100174.
HGNC	HGNC:27622. FRRS1.
HPA	HPA017883.
MIM	611578. gene.
neXtProt	NX_Q6ZNA5.
PharmGKB	PA142670941.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG281275.
HOGENOM	HOG000112648.
HOVERGEN	HBG107929.
OMA	PGPIISQ.
Gene expression databases
Bgee	Q6ZNA5.
CleanEx	HS_FRRS1.
Genevestigator	Q6ZNA5.
Family and domain databases
InterPro	IPR006593. Cyt_b561/ferric_Rdtase_TM. IPR005018. DOMON_domain. IPR002861. Reeler_dom. [Graphical view]
Pfam	PF03351. DOMON. 1 hit. PF02014. Reeler. 1 hit. [Graphical view]
SMART	SM00665. B561. 1 hit. SM00664. DoH. 1 hit. [Graphical view]
PROSITE	PS50939. CYTOCHROME_B561. 1 hit. PS50836. DOMON. 1 hit. PS51019. REELIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	391059.
NextBio	104295.
SOURCE	Search...

Entry information

Entry name

FRRS1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.