S5A1_HUMAN
ID S5A1_HUMAN Reviewed; 259 AA.
AC P18405; B2R7Q1; Q9UHY4; Q9UP36; Q9UP37;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 1;
DE EC=1.3.1.22 {ECO:0000269|PubMed:2339109};
DE AltName: Full=SR type 1;
DE AltName: Full=Steroid 5-alpha-reductase 1;
DE Short=S5AR 1;
GN Name=SRD5A1 {ECO:0000312|HGNC:HGNC:11284};
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 [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2339109; DOI=10.1073/pnas.87.10.3640;
RA Andersson S., Russell D.W.;
RT "Structural and biochemical properties of cloned and expressed human and
RT rat steroid 5 alpha-reductases.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3640-3644(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1686016; DOI=10.1016/0888-7543(91)90038-g;
RA Jenkins E.P., Hsieh C.L., Milatovich A., Normington K., Berman D.M.,
RA Francke U., Russell D.W.;
RT "Characterization and chromosomal mapping of a human steroid 5 alpha-
RT reductase gene and pseudogene and mapping of the mouse homologue.";
RL Genomics 11:1102-1112(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Urinary bladder;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 AND 155-187.
RX PubMed=11678334; DOI=10.1007/s004240100019;
RA Eminovic I., Liovic M., Prezelj J., Kocijancic A., Rozman D., Komel R.;
RT "New steroid 5alpha-reductase type I (SRD5A1) homologous sequences on human
RT chromosomes 6 and 8.";
RL Pflugers Arch. 442:R187-R189(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and
CC progesterone or corticosterone into their corresponding 5-alpha-3-
CC oxosteroids. It plays a central role in sexual differentiation and
CC androgen physiology. {ECO:0000269|PubMed:2339109}.
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:0000269|PubMed:2339109};
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:2339109};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50817;
CC Evidence={ECO:0000305|PubMed:2339109};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-pregnane-3,20-dione + NADP(+) = H(+) + NADPH +
CC progesterone; Xref=Rhea:RHEA:21952, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:28952, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000269|PubMed:2339109};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954;
CC Evidence={ECO:0000305|PubMed:2339109};
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:2339109};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC Evidence={ECO:0000305|PubMed:2339109};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for testosterone {ECO:0000269|PubMed:2339109};
CC KM=1.7 uM for androstenedione {ECO:0000269|PubMed:2339109};
CC KM=0.8 uM for progesterone {ECO:0000269|PubMed:2339109};
CC Vmax=3.6 nmol/min/mg enzyme toward testosterone
CC {ECO:0000269|PubMed:2339109};
CC Vmax=5.3 nmol/min/mg enzyme toward androstenedione
CC {ECO:0000269|PubMed:2339109};
CC Vmax=5.0 nmol/min/mg enzyme toward progesterone
CC {ECO:0000269|PubMed:2339109};
CC pH dependence:
CC Optimally active at alkaline pHs.;
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Liver and prostate (at a low level).
CC -!- INDUCTION: Its expression is regulated by androgens such as
CC testosterone.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/srd5a1/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=5-alpha reductase entry;
CC URL="https://en.wikipedia.org/wiki/5_alpha_reductase";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32313; AAA35490.1; -; mRNA.
DR EMBL; M68886; AAA60995.1; -; Genomic_DNA.
DR EMBL; M68882; AAA60995.1; JOINED; Genomic_DNA.
DR EMBL; M68883; AAA60995.1; JOINED; Genomic_DNA.
DR EMBL; M68884; AAA60995.1; JOINED; Genomic_DNA.
DR EMBL; M68885; AAA60995.1; JOINED; Genomic_DNA.
DR EMBL; AF052126; AAC28620.1; -; mRNA.
DR EMBL; AF113128; AAF14869.1; -; mRNA.
DR EMBL; BT006834; AAP35480.1; -; mRNA.
DR EMBL; AY341029; AAP88935.1; -; Genomic_DNA.
DR EMBL; AK313070; BAG35898.1; -; mRNA.
DR EMBL; CH471102; EAX08104.1; -; Genomic_DNA.
DR EMBL; BC007033; AAH07033.1; -; mRNA.
DR EMBL; BC008673; AAH08673.1; -; mRNA.
DR EMBL; AF073301; AAC26862.1; -; Genomic_DNA.
DR EMBL; AF073302; AAC26863.1; -; Genomic_DNA.
DR EMBL; AF073303; AAC26864.1; -; Genomic_DNA.
DR EMBL; AF073304; AAC26865.1; -; Genomic_DNA.
DR CCDS; CCDS3870.1; -.
DR PIR; A55274; A55274.
DR RefSeq; NP_001038.1; NM_001047.3.
DR RefSeq; NP_001311251.1; NM_001324322.1.
DR RefSeq; NP_001311252.1; NM_001324323.1.
DR AlphaFoldDB; P18405; -.
DR SMR; P18405; -.
DR BioGRID; 112593; 18.
DR IntAct; P18405; 2.
DR STRING; 9606.ENSP00000274192; -.
DR BindingDB; P18405; -.
DR ChEMBL; CHEMBL1787; -.
DR DrugBank; DB01126; Dutasteride.
DR DrugBank; DB01216; Finasteride.
DR DrugBank; DB00367; Levonorgestrel.
DR DrugBank; DB00717; Norethisterone.
DR DrugBank; DB09389; Norgestrel.
DR DrugBank; DB06412; Oxymetholone.
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 DrugCentral; P18405; -.
DR SwissLipids; SLP:000001636; -.
DR iPTMnet; P18405; -.
DR PhosphoSitePlus; P18405; -.
DR BioMuta; SRD5A1; -.
DR DMDM; 134151; -.
DR EPD; P18405; -.
DR MassIVE; P18405; -.
DR MaxQB; P18405; -.
DR PaxDb; P18405; -.
DR PeptideAtlas; P18405; -.
DR PRIDE; P18405; -.
DR ProteomicsDB; 53557; -.
DR Antibodypedia; 22401; 182 antibodies from 32 providers.
DR DNASU; 6715; -.
DR Ensembl; ENST00000274192.7; ENSP00000274192.5; ENSG00000145545.12.
DR GeneID; 6715; -.
DR KEGG; hsa:6715; -.
DR MANE-Select; ENST00000274192.7; ENSP00000274192.5; NM_001047.4; NP_001038.1.
DR UCSC; uc003jdw.4; human.
DR CTD; 6715; -.
DR DisGeNET; 6715; -.
DR GeneCards; SRD5A1; -.
DR HGNC; HGNC:11284; SRD5A1.
DR HPA; ENSG00000145545; Tissue enhanced (liver).
DR MIM; 184753; gene.
DR neXtProt; NX_P18405; -.
DR OpenTargets; ENSG00000145545; -.
DR PharmGKB; PA36112; -.
DR VEuPathDB; HostDB:ENSG00000145545; -.
DR eggNOG; KOG1638; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_065395_1_1_1; -.
DR InParanoid; P18405; -.
DR OMA; SQHAVYA; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; P18405; -.
DR TreeFam; TF314668; -.
DR BioCyc; MetaCyc:HS07261-MON; -.
DR BRENDA; 1.3.1.22; 2681.
DR BRENDA; 1.3.99.5; 2681.
DR PathwayCommons; P18405; -.
DR Reactome; R-HSA-193048; Androgen biosynthesis.
DR SignaLink; P18405; -.
DR SIGNOR; P18405; -.
DR BioGRID-ORCS; 6715; 10 hits in 1066 CRISPR screens.
DR GeneWiki; SRD5A1; -.
DR GenomeRNAi; 6715; -.
DR Pharos; P18405; Tclin.
DR PRO; PR:P18405; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P18405; protein.
DR Bgee; ENSG00000145545; Expressed in esophagus squamous epithelium and 176 other tissues.
DR ExpressionAtlas; P18405; baseline and differential.
DR Genevisible; P18405; HS.
DR GO; GO:0070852; C:cell body fiber; IEA:Ensembl.
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:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0033218; F:amide binding; IEA:Ensembl.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050213; F:progesterone 5-alpha-reductase activity; IEA:RHEA.
DR GO; GO:0006702; P:androgen biosynthetic process; TAS:Reactome.
DR GO; GO:0006710; P:androgen catabolic process; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0042747; P:circadian sleep/wake cycle, REM sleep; IEA:Ensembl.
DR GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
DR GO; GO:0030540; P:female genitalia development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl.
DR GO; GO:0007530; P:sex determination; NAS:ProtInc.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Microsome; NADP; Oxidoreductase; Reference proteome;
KW Sexual differentiation; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase 1"
FT /id="PRO_0000213674"
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 29..76
FT /note="Missing (in Ref. 4; AAF14869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29459 MW; AEF9FD5521E43AC4 CRC64;
MATATGVAEE RLLAALAYLQ CAVGCAVFAR NRQTNSVYGR HALPSHRLRV PARAAWVVQE
LPSLALPLYQ YASESAPRLR SAPNCILLAM FLVHYGHRCL IYPFLMRGGK PMPLLACTMA
IMFCTCNGYL QSRYLSHCAV YADDWVTDPR FLIGFGLWLT GMLINIHSDH ILRNLRKPGD
TGYKIPRGGL FEYVTAANYF GEIMEWCGYA LASWSVQGAA FAFFTFCFLS GRAKEHHEWY
LRKFEEYPKF RKIIIPFLF
