PORED_HUMAN
ID PORED_HUMAN Reviewed; 318 AA.
AC Q9H8P0; Q4W5Q6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Polyprenol reductase {ECO:0000305};
DE EC=1.3.1.94 {ECO:0000269|PubMed:20637498};
DE AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3;
DE EC=1.3.1.22 {ECO:0000269|PubMed:26855069};
DE AltName: Full=Steroid 5-alpha-reductase 2-like;
DE AltName: Full=Steroid 5-alpha-reductase 3;
DE Short=S5AR 3;
DE Short=SR type 3;
GN Name=SRD5A3 {ECO:0000303|PubMed:17986282, ECO:0000312|HGNC:HGNC:25812};
GN Synonyms=SRD5A2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-296.
RX PubMed=17986282; DOI=10.1111/j.1349-7006.2007.00656.x;
RA Uemura M., Tamura K., Chung S., Honma S., Okuyama A., Nakamura Y.,
RA Nakagawa H.;
RT "Novel 5 alpha-steroid reductase (SRD5A3, type-3) is overexpressed in
RT hormone-refractory prostate cancer.";
RL Cancer Sci. 99:81-86(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INVOLVEMENT IN
RP CDG1Q, AND MUTAGENESIS OF HIS-296.
RX PubMed=20637498; DOI=10.1016/j.cell.2010.06.001;
RA Cantagrel V., Lefeber D.J., Ng B.G., Guan Z., Silhavy J.L., Bielas S.L.,
RA Lehle L., Hombauer H., Adamowicz M., Swiezewska E., De Brouwer A.P.,
RA Blumel P., Sykut-Cegielska J., Houliston S., Swistun D., Ali B.R.,
RA Dobyns W.B., Babovic-Vuksanovic D., van Bokhoven H., Wevers R.A.,
RA Raetz C.R., Freeze H.H., Morava E., Al-Gazali L., Gleeson J.G.;
RT "SRD5A3 is required for converting polyprenol to dolichol and is mutated in
RT a congenital glycosylation disorder.";
RL Cell 142:203-217(2010).
RN [8]
RP INVOLVEMENT IN KHRZ.
RX PubMed=20700148; DOI=10.1038/ejhg.2010.132;
RA Kahrizi K., Hu C.H., Garshasbi M., Abedini S.S., Ghadami S.,
RA Kariminejad R., Ullmann R., Chen W., Ropers H.H., Kuss A.W., Najmabadi H.,
RA Tzschach A.;
RT "Next generation sequencing in a family with autosomal recessive Kahrizi
RT syndrome (OMIM 612713) reveals a homozygous frameshift mutation in
RT SRD5A3.";
RL Eur. J. Hum. Genet. 19:115-117(2011).
RN [9]
RP INVOLVEMENT IN CDG1Q.
RX PubMed=22240719; DOI=10.1016/j.ejpn.2011.12.011;
RA Kasapkara C.S., Tumer L., Ezgu F.S., Hasanoglu A., Race V., Matthijs G.,
RA Jaeken J.;
RT "SRD5A3-CDG: A patient with a novel mutation.";
RL Eur. J. Paediatr. Neurol. 16:554-556(2012).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=26855069; DOI=10.1016/j.jsbmb.2016.02.003;
RA Fouad Mansour M., Pelletier M., Tchernof A.;
RT "Characterization of 5alpha-reductase activity and isoenzymes in human
RT abdominal adipose tissues.";
RL J. Steroid Biochem. Mol. Biol. 161:45-53(2016).
CC -!- FUNCTION: Plays a key role in early steps of protein N-linked
CC glycosylation by being required for the conversion of polyprenol into
CC dolichol (PubMed:20637498). Dolichols are required for the synthesis of
CC dolichol-linked monosaccharides and the oligosaccharide precursor used
CC for N-glycosylation (PubMed:20637498). Acts as a polyprenol reductase
CC that promotes the reduction of the alpha-isoprene unit of polyprenols
CC into dolichols in a NADP-dependent mechanism (PubMed:20637498). Also
CC able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT)
CC (PubMed:17986282, PubMed:26855069). {ECO:0000269|PubMed:17986282,
CC ECO:0000269|PubMed:20637498, ECO:0000269|PubMed:26855069}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol
CC + H(+) + NADPH; Xref=Rhea:RHEA:34279, Rhea:RHEA-COMP:9521, Rhea:RHEA-
CC COMP:9525, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:67132; EC=1.3.1.94;
CC Evidence={ECO:0000269|PubMed:20637498};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281;
CC Evidence={ECO:0000305|PubMed:20637498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000305|PubMed:26855069};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC Evidence={ECO:0000305|PubMed:26855069};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha-androstan-
CC 3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:26855069};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC Evidence={ECO:0000305|PubMed:26855069};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH
CC + testosterone; Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000269|PubMed:26855069};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC Evidence={ECO:0000305|PubMed:26855069};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:20637498}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:20637498}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:20637498}.
CC -!- TISSUE SPECIFICITY: Expressed in preadipocytes (at protein level)
CC (PubMed:26855069). Overexpressed in hormone-refractory prostate cancers
CC (HRPC). Almost no or little expression in normal adult organs.
CC {ECO:0000269|PubMed:17986282, ECO:0000269|PubMed:26855069}.
CC -!- DISEASE: Congenital disorder of glycosylation 1Q (CDG1Q) [MIM:612379]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:20637498,
CC ECO:0000269|PubMed:22240719}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Kahrizi syndrome (KHRZ) [MIM:612713]: An autosomal recessive
CC neurodevelopmental disorder characterized by intellectual disability,
CC cataracts, coloboma, kyphosis, and coarse facial features.
CC {ECO:0000269|PubMed:20700148}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; AK023414; BAB14568.1; -; mRNA.
DR EMBL; CR457312; CAG33593.1; -; mRNA.
DR EMBL; AC064824; AAY40904.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05465.1; -; Genomic_DNA.
DR EMBL; BC002480; AAH02480.1; -; mRNA.
DR CCDS; CCDS3498.1; -.
DR RefSeq; NP_078868.1; NM_024592.4.
DR AlphaFoldDB; Q9H8P0; -.
DR SMR; Q9H8P0; -.
DR BioGRID; 122772; 5.
DR IntAct; Q9H8P0; 2.
DR STRING; 9606.ENSP00000264228; -.
DR ChEMBL; CHEMBL2363075; -.
DR DrugBank; DB00717; Norethisterone.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB01420; Testosterone propionate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR SwissLipids; SLP:000001637; -.
DR iPTMnet; Q9H8P0; -.
DR PhosphoSitePlus; Q9H8P0; -.
DR BioMuta; SRD5A3; -.
DR DMDM; 74733864; -.
DR jPOST; Q9H8P0; -.
DR MassIVE; Q9H8P0; -.
DR MaxQB; Q9H8P0; -.
DR PaxDb; Q9H8P0; -.
DR PeptideAtlas; Q9H8P0; -.
DR PRIDE; Q9H8P0; -.
DR ProteomicsDB; 81231; -.
DR Antibodypedia; 12328; 81 antibodies from 19 providers.
DR DNASU; 79644; -.
DR Ensembl; ENST00000264228.9; ENSP00000264228.4; ENSG00000128039.13.
DR GeneID; 79644; -.
DR KEGG; hsa:79644; -.
DR MANE-Select; ENST00000264228.9; ENSP00000264228.4; NM_024592.5; NP_078868.1.
DR UCSC; uc003hau.4; human.
DR CTD; 79644; -.
DR DisGeNET; 79644; -.
DR GeneCards; SRD5A3; -.
DR GeneReviews; SRD5A3; -.
DR HGNC; HGNC:25812; SRD5A3.
DR HPA; ENSG00000128039; Low tissue specificity.
DR MalaCards; SRD5A3; -.
DR MIM; 611715; gene.
DR MIM; 612379; phenotype.
DR MIM; 612713; phenotype.
DR neXtProt; NX_Q9H8P0; -.
DR OpenTargets; ENSG00000128039; -.
DR Orphanet; 324737; SRD5A3-CDG.
DR PharmGKB; PA162404779; -.
DR VEuPathDB; HostDB:ENSG00000128039; -.
DR eggNOG; KOG1640; Eukaryota.
DR GeneTree; ENSGT00500000044920; -.
DR HOGENOM; CLU_044409_2_1_1; -.
DR InParanoid; Q9H8P0; -.
DR OMA; SSPHMFF; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q9H8P0; -.
DR TreeFam; TF315011; -.
DR BioCyc; MetaCyc:HS13249-MON; -.
DR BRENDA; 1.3.1.22; 2681.
DR BRENDA; 1.3.1.94; 2681.
DR BRENDA; 1.3.1.B13; 2681.
DR PathwayCommons; Q9H8P0; -.
DR Reactome; R-HSA-193048; Androgen biosynthesis.
DR Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR Reactome; R-HSA-4755579; Defective SRD5A3 causes SRD5A3-CDG, KHRZ.
DR SignaLink; Q9H8P0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79644; 67 hits in 1076 CRISPR screens.
DR ChiTaRS; SRD5A3; human.
DR GeneWiki; SRD5A3; -.
DR GenomeRNAi; 79644; -.
DR Pharos; Q9H8P0; Tbio.
DR PRO; PR:Q9H8P0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H8P0; protein.
DR Bgee; ENSG00000128039; Expressed in palpebral conjunctiva and 163 other tissues.
DR ExpressionAtlas; Q9H8P0; baseline and differential.
DR Genevisible; Q9H8P0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006702; P:androgen biosynthetic process; TAS:Reactome.
DR GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
DR GO; GO:0019348; P:dolichol metabolic process; IDA:UniProtKB.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006489; P:dolichyl diphosphate biosynthetic process; TAS:Reactome.
DR GO; GO:0016095; P:polyprenol catabolic process; IDA:UniProtKB.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039698; Dfg10/SRD5A3.
DR PANTHER; PTHR14624; PTHR14624; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Cataract; Congenital disorder of glycosylation; Endoplasmic reticulum;
KW Intellectual disability; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Polyprenol reductase"
FT /id="PRO_0000317703"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..80
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..157
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..260
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 296
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:17986282,
FT ECO:0000269|PubMed:20637498"
SQ SEQUENCE 318 AA; 36521 MW; 404C7ECBB4A29E6B CRC64;
MAPWAEAEHS ALNPLRAVWL TLTAAFLLTL LLQLLPPGLL PGCAIFQDLI RYGKTKCGEP
SRPAACRAFD VPKRYFSHFY IISVLWNGFL LWCLTQSLFL GAPFPSWLHG LLRILGAAQF
QGGELALSAF LVLVFLWLHS LRRLFECLYV SVFSNVMIHV VQYCFGLVYY VLVGLTVLSQ
VPMDGRNAYI TGKNLLMQAR WFHILGMMMF IWSSAHQYKC HVILGNLRKN KAGVVIHCNH
RIPFGDWFEY VSSPNYLAEL MIYVSMAVTF GFHNLTWWLV VTNVFFNQAL SAFLSHQFYK
SKFVSYPKHR KAFLPFLF
