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Q96K12

- FACR2_HUMAN

UniProt

Q96K12 - FACR2_HUMAN

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Protein

Fatty acyl-CoA reductase 2

Gene

FAR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates.1 Publication

Catalytic activityi

Hexadecanal + CoA + NADP+ = hexadecanoyl-CoA + NADPH.

GO - Molecular functioni

  1. fatty-acyl-CoA reductase (alcohol-forming) activity Source: UniProtKB
  2. long-chain-fatty-acyl-CoA reductase activity Source: Ensembl

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. ether lipid biosynthetic process Source: Reactome
  3. long-chain fatty-acyl-CoA metabolic process Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_1407. Plasmalogen biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acyl-CoA reductase 2 (EC:1.2.1.n2)
Alternative name(s):
Male sterility domain-containing protein 1
Gene namesi
Name:FAR2
Synonyms:MLSTD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:25531. FAR2.

Subcellular locationi

Peroxisome membrane Curated; Multi-pass membrane protein Curated. Endoplasmic reticulum membrane Curated; Multi-pass membrane protein Curated
Note: Peroxisome in cells expressing low levels of the protein. Peroxisome and endoplasmic reticulum in cells expressing high levels of the protein.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei465 – 48420HelicalSequence AnalysisAdd
BLAST
Transmembranei491 – 51020HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. peroxisomal matrix Source: Reactome
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388036.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Fatty acyl-CoA reductase 2PRO_0000261401Add
BLAST

Proteomic databases

MaxQBiQ96K12.
PaxDbiQ96K12.
PRIDEiQ96K12.

PTM databases

PhosphoSiteiQ96K12.

Expressioni

Gene expression databases

BgeeiQ96K12.
CleanExiHS_FAR2.
ExpressionAtlasiQ96K12. baseline and differential.
GenevestigatoriQ96K12.

Organism-specific databases

HPAiHPA015884.

Interactioni

Protein-protein interaction databases

BioGridi120834. 7 interactions.
STRINGi9606.ENSP00000182377.

Structurei

3D structure databases

ProteinModelPortaliQ96K12.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the fatty acyl-CoA reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG325153.
GeneTreeiENSGT00390000006367.
HOGENOMiHOG000261667.
HOVERGENiHBG076152.
InParanoidiQ96K12.
KOiK13356.
OMAiNIHYLFN.
PhylomeDBiQ96K12.
TreeFamiTF313011.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR026055. FAR.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11011. PTHR11011. 1 hit.
PfamiPF07993. NAD_binding_4. 1 hit.
PF03015. Sterile. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96K12-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSTIAAFYGG KSILITGATG FLGKVLMEKL FRTSPDLKVI YILVRPKAGQ
60 70 80 90 100
TLQQRVFQIL DSKLFEKVKE VCPNVHEKIR AIYADLNQND FAISKEDMQE
110 120 130 140 150
LLSCTNIIFH CAATVRFDDT LRHAVQLNVT ATRQLLLMAS QMPKLEAFIH
160 170 180 190 200
ISTAYSNCNL KHIDEVIYPC PVEPKKIIDS LEWLDDAIID EITPKLIRDW
210 220 230 240 250
PNIYTYTKAL GEMVVQQESR NLNIAIIRPS IVGATWQEPF PGWVDNINGP
260 270 280 290 300
NGIIIATGKG FLRAIKATPM AVADVIPVDT VVNLMLAVGW YTAVHRPKST
310 320 330 340 350
LVYHITSGNM NPCNWHKMGV QVLATFEKIP FERPFRRPNA NFTSNSFTSQ
360 370 380 390 400
YWNAVSHRAP AIIYDCYLRL TGRKPRMTKL MNRLLRTVSM LEYFINRSWE
410 420 430 440 450
WSTYNTEMLM SELSPEDQRV FNFDVRQLNW LEYIENYVLG VKKYLLKEDM
460 470 480 490 500
AGIPKAKQRL KRLRNIHYLF NTALFLIAWR LLIARSQMAR NVWFFIVSFC
510
YKFLSYFRAS STLKV
Length:515
Mass (Da):59,438
Last modified:December 1, 2001 - v1
Checksum:i6EFC67ED29796094
GO
Isoform 2 (identifier: Q96K12-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Note: No experimental confirmation available.

Show »
Length:418
Mass (Da):48,537
Checksum:iD3C00E8A95635C5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511T → A in CAB66777. (PubMed:11230166)Curated
Sequence conflicti167 – 1671I → T in BAA91625. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261F → S.
Corresponds to variant rs17400011 [ dbSNP | Ensembl ].
VAR_053801
Natural varianti329 – 3291I → T.
Corresponds to variant rs17404064 [ dbSNP | Ensembl ].
VAR_053802

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_055648Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136843 mRNA. Translation: CAB66777.1.
AK001324 mRNA. Translation: BAA91625.1.
AK027756 mRNA. Translation: BAB55347.1.
AK129857 mRNA. No translation available.
AC009318 Genomic DNA. No translation available.
AC012150 Genomic DNA. No translation available.
BC022267 mRNA. Translation: AAH22267.1.
CCDSiCCDS61084.1. [Q96K12-2]
CCDS8717.1. [Q96K12-1]
RefSeqiNP_001258712.1. NM_001271783.1. [Q96K12-1]
NP_060569.3. NM_018099.4. [Q96K12-1]
UniGeneiHs.728955.
Hs.744741.

Genome annotation databases

EnsembliENST00000182377; ENSP00000182377; ENSG00000064763. [Q96K12-1]
ENST00000536681; ENSP00000443291; ENSG00000064763. [Q96K12-1]
ENST00000547116; ENSP00000449349; ENSG00000064763. [Q96K12-2]
GeneIDi55711.
KEGGihsa:55711.
UCSCiuc001ris.5. human. [Q96K12-1]

Polymorphism databases

DMDMi74732166.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136843 mRNA. Translation: CAB66777.1 .
AK001324 mRNA. Translation: BAA91625.1 .
AK027756 mRNA. Translation: BAB55347.1 .
AK129857 mRNA. No translation available.
AC009318 Genomic DNA. No translation available.
AC012150 Genomic DNA. No translation available.
BC022267 mRNA. Translation: AAH22267.1 .
CCDSi CCDS61084.1. [Q96K12-2 ]
CCDS8717.1. [Q96K12-1 ]
RefSeqi NP_001258712.1. NM_001271783.1. [Q96K12-1 ]
NP_060569.3. NM_018099.4. [Q96K12-1 ]
UniGenei Hs.728955.
Hs.744741.

3D structure databases

ProteinModelPortali Q96K12.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120834. 7 interactions.
STRINGi 9606.ENSP00000182377.

PTM databases

PhosphoSitei Q96K12.

Polymorphism databases

DMDMi 74732166.

Proteomic databases

MaxQBi Q96K12.
PaxDbi Q96K12.
PRIDEi Q96K12.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000182377 ; ENSP00000182377 ; ENSG00000064763 . [Q96K12-1 ]
ENST00000536681 ; ENSP00000443291 ; ENSG00000064763 . [Q96K12-1 ]
ENST00000547116 ; ENSP00000449349 ; ENSG00000064763 . [Q96K12-2 ]
GeneIDi 55711.
KEGGi hsa:55711.
UCSCi uc001ris.5. human. [Q96K12-1 ]

Organism-specific databases

CTDi 55711.
GeneCardsi GC12P029302.
H-InvDB HIX0010513.
HGNCi HGNC:25531. FAR2.
HPAi HPA015884.
neXtProti NX_Q96K12.
PharmGKBi PA162388036.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG325153.
GeneTreei ENSGT00390000006367.
HOGENOMi HOG000261667.
HOVERGENi HBG076152.
InParanoidi Q96K12.
KOi K13356.
OMAi NIHYLFN.
PhylomeDBi Q96K12.
TreeFami TF313011.

Enzyme and pathway databases

Reactomei REACT_1407. Plasmalogen biosynthesis.

Miscellaneous databases

GenomeRNAii 55711.
NextBioi 35511747.
PROi Q96K12.

Gene expression databases

Bgeei Q96K12.
CleanExi HS_FAR2.
ExpressionAtlasi Q96K12. baseline and differential.
Genevestigatori Q96K12.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR026055. FAR.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11011. PTHR11011. 1 hit.
Pfami PF07993. NAD_binding_4. 1 hit.
PF03015. Sterile. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Heart, Placenta and Teratocarcinoma.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1).
    Tissue: Placenta.
  5. "Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A reductases with different substrate specificities and tissue distributions."
    Cheng J.B., Russell D.W.
    J. Biol. Chem. 279:37789-37797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiFACR2_HUMAN
AccessioniPrimary (citable) accession number: Q96K12
Secondary accession number(s): F8VV73, Q9H0D5, Q9NVW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3