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HSDD1_ARATH
ID   HSDD1_ARATH             Reviewed;         439 AA.
AC   Q9FX01; Q0VH36; Q8LER8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 {ECO:0000303|PubMed:16835224};
DE            Short=At3BETAHSD/D1 {ECO:0000303|PubMed:16835224};
DE            EC=1.1.1.418 {ECO:0000269|PubMed:16835224, ECO:0000269|PubMed:19218365};
DE   AltName: Full=4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-1;
DE   AltName: Full=Reticulon-like protein B24 {ECO:0000303|PubMed:17604024};
DE            Short=AtRTNLB24 {ECO:0000303|PubMed:17604024};
DE   AltName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase 1, decarboxylating;
GN   Name=3BETAHSD/D1 {ECO:0000303|PubMed:16835224};
GN   Synonyms=RTNLB24 {ECO:0000303|PubMed:17604024};
GN   OrderedLocusNames=At1g47290 {ECO:0000312|Araport:AT1G47290};
GN   ORFNames=T3F24.9 {ECO:0000312|EMBL:AAG11424.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP   PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=16835224; DOI=10.1074/jbc.m604431200;
RA   Rahier A., Darnet S., Bouvier F., Camara B., Bard M.;
RT   "Molecular and enzymatic characterizations of novel bifunctional 3beta-
RT   hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis
RT   thaliana.";
RL   J. Biol. Chem. 281:27264-27277(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17604024; DOI=10.1016/j.febslet.2007.06.032;
RA   Nziengui H., Bouhidel K., Pillon D., Der C., Marty F., Schoefs B.;
RT   "Reticulon-like proteins in Arabidopsis thaliana: structural organization
RT   and ER localization.";
RL   FEBS Lett. 581:3356-3362(2007).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF ASP-41; ASP-72; THR-131; SER-133; SER-135;
RP   TYR-161; LYS-165; ARG-320 AND ARG-328, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=19218365; DOI=10.1104/pp.108.132282;
RA   Rahier A., Bergdoll M., Genot G., Bouvier F., Camara B.;
RT   "Homology modeling and site-directed mutagenesis reveal catalytic key amino
RT   acids of 3beta-hydroxysteroid-dehydrogenase/C4-decarboxylase from
RT   Arabidopsis.";
RL   Plant Physiol. 149:1872-1886(2009).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=22673766; DOI=10.1007/s10059-012-0102-6;
RA   Kim B., Kim G., Fujioka S., Takatsuto S., Choe S.;
RT   "Overexpression of 3beta-hydroxysteroid dehydrogenases/C-4 decarboxylases
RT   causes growth defects possibly due to abnormal auxin transport in
RT   Arabidopsis.";
RL   Mol. Cells 34:77-84(2012).
CC   -!- FUNCTION: 3beta-hydroxysteroid-dehydrogenase/decarboxylase involved in
CC       sterol synthesis (PubMed:16835224). Catalyzes the formation of 3-
CC       oxosteroids from 3beta-hydroxysteroids-4alpha-carboxylate
CC       (PubMed:16835224). Involved in the regulation of inflorescence
CC       internodes and leaves growth, probably by affecting auxin transporter
CC       activity possibly by altering sterol composition in the membranes
CC       (PubMed:22673766). {ECO:0000269|PubMed:16835224,
CC       ECO:0000269|PubMed:22673766}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxysteroid-4alpha-carboxylate + NAD(+) = a 3-
CC         oxosteroid + CO2 + NADH; Xref=Rhea:RHEA:34775, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:136966; EC=1.1.1.418;
CC         Evidence={ECO:0000269|PubMed:16835224, ECO:0000269|PubMed:19218365};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4alpha-carboxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-
CC         ergost-24(24(1))-en-3beta-ol + NAD(+) = CO2 + cycloeucalenone + NADH;
CC         Xref=Rhea:RHEA:59016, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:142915, ChEBI:CHEBI:142916;
CC         EC=1.1.1.418; Evidence={ECO:0000269|PubMed:16835224,
CC         ECO:0000269|PubMed:19218365};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.13 mM for 4alpha-carboxy-5alpha-cholest-7-en-3beta-ol
CC         {ECO:0000269|PubMed:19218365};
CC         KM=0.26 mM for 4alpha-carboxy-4beta-methyl-5alpha-cholest-8,24-dien-
CC         3beta-ol {ECO:0000269|PubMed:19218365};
CC         KM=134 uM for 4alpha-carboxy-cholest-7-en-3beta-ol
CC         {ECO:0000269|PubMed:16835224};
CC         KM=112 uM for 3alpha-deutero-4alpha-carboxy-cholest-7-en-3beta-ol
CC         {ECO:0000269|PubMed:16835224};
CC         KM=383 uM for 4alpha-carboxy-cholest-7-en-3alpha-ol
CC         {ECO:0000269|PubMed:16835224};
CC         KM=274 uM for 4alpha-carboxy-4beta-methyl-cholest-8,24-dien-3beta-ol
CC         {ECO:0000269|PubMed:16835224};
CC         KM=8 uM for NAD(+) {ECO:0000269|PubMed:16835224};
CC         Vmax=88 nmol/h/mg enzyme with 4alpha-carboxy-5alpha-cholest-7-en-
CC         3beta-ol as substrate {ECO:0000269|PubMed:19218365};
CC         Vmax=111 nmol/h/mg enzyme with 4alpha-carboxy-4beta-methyl-5alpha-
CC         cholest-8,24-dien-3beta-ol as substrate
CC         {ECO:0000269|PubMed:19218365};
CC         Vmax=86 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3beta-ol as
CC         substrate {ECO:0000269|PubMed:16835224};
CC         Vmax=77 nmol/h/mg enzyme with 3alpha-deutero-4alpha-carboxy-cholest-
CC         7-en-3beta-ol as substrate {ECO:0000269|PubMed:16835224};
CC         Vmax=5.7 nmol/h/mg enzyme with 4alpha-carboxy-cholest-7-en-3alpha-ol
CC         as substrate {ECO:0000269|PubMed:16835224};
CC         Vmax=113 nmol/h/mg enzyme with 4alpha-carboxy-4beta-methyl-cholest-
CC         8,24-dien-3beta-ol as substrate {ECO:0000269|PubMed:16835224};
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 4/6. {ECO:0000269|PubMed:16835224}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O43050}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FX01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FX01-2; Sequence=VSP_037002;
CC   -!- DOMAIN: The RETICULON domain is partial in comparison with the other
CC       paralogs.
CC   -!- DISRUPTION PHENOTYPE: No noticeable phenotype.
CC       {ECO:0000269|PubMed:22673766}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC   -!- CAUTION: Lacks one transmembrane, which is a conserved feature of the
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM62504.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAY28502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- SEQUENCE CAUTION: [Isoform 2]:
CC       Sequence=AAM62504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAY28502.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY957470; AAY28502.1; ALT_INIT; mRNA.
DR   EMBL; AC015449; AAG11424.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32152.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32153.1; -; Genomic_DNA.
DR   EMBL; AK117478; BAC42142.1; -; mRNA.
DR   EMBL; BT005166; AAO50699.1; -; mRNA.
DR   EMBL; AY085272; AAM62504.1; ALT_INIT; mRNA.
DR   PIR; F96513; F96513.
DR   RefSeq; NP_564502.1; NM_103623.5. [Q9FX01-2]
DR   RefSeq; NP_849779.1; NM_179448.4. [Q9FX01-1]
DR   AlphaFoldDB; Q9FX01; -.
DR   SMR; Q9FX01; -.
DR   BioGRID; 26357; 4.
DR   IntAct; Q9FX01; 2.
DR   STRING; 3702.AT1G47290.2; -.
DR   PaxDb; Q9FX01; -.
DR   PRIDE; Q9FX01; -.
DR   ProteomicsDB; 232129; -. [Q9FX01-1]
DR   EnsemblPlants; AT1G47290.1; AT1G47290.1; AT1G47290. [Q9FX01-2]
DR   EnsemblPlants; AT1G47290.2; AT1G47290.2; AT1G47290. [Q9FX01-1]
DR   GeneID; 841132; -.
DR   Gramene; AT1G47290.1; AT1G47290.1; AT1G47290. [Q9FX01-2]
DR   Gramene; AT1G47290.2; AT1G47290.2; AT1G47290. [Q9FX01-1]
DR   KEGG; ath:AT1G47290; -.
DR   Araport; AT1G47290; -.
DR   TAIR; locus:2203771; AT1G47290.
DR   eggNOG; KOG1430; Eukaryota.
DR   InParanoid; Q9FX01; -.
DR   OMA; VTNDEHI; -.
DR   OrthoDB; 930591at2759; -.
DR   PhylomeDB; Q9FX01; -.
DR   BioCyc; ARA:AT1G47290-MON; -.
DR   BioCyc; MetaCyc:AT1G47290-MON; -.
DR   BRENDA; 1.1.1.418; 399.
DR   UniPathway; UPA00770; UER00757.
DR   PRO; PR:Q9FX01; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FX01; baseline and differential.
DR   Genevisible; Q9FX01; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0102175; F:3-beta-hydroxysteroid dehydrogenase/C4-decarboxylase activity; IEA:RHEA.
DR   GO; GO:0102191; F:4alpha-carboxy-5alpha-cholesta-7,24-dien-3beta-ol dehydrogenase/C4-decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0047012; F:sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating) activity; IDA:TAIR.
DR   GO; GO:0060918; P:auxin transport; IMP:UniProtKB.
DR   GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR   GO; GO:0032409; P:regulation of transporter activity; IMP:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..439
FT                   /note="3beta-hydroxysteroid-dehydrogenase/decarboxylase
FT                   isoform 1"
FT                   /id="PRO_0000371279"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          371..439
FT                   /note="Reticulon; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
FT   BINDING         16..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q12068"
FT   SITE            41
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   SITE            72
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   SITE            131
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   SITE            161
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   SITE            165
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   SITE            328
FT                   /note="Essential for the 3betaHSD/D activity"
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         371..427
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16835224, ECO:0000303|Ref.6"
FT                   /id="VSP_037002"
FT   MUTAGEN         41
FT                   /note="D->V: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         72
FT                   /note="D->A,V: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         131
FT                   /note="T->V: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         133
FT                   /note="S->A: Reduced activity with slower catalysis and
FT                   lower substrate binding."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         135
FT                   /note="S->A: Normal activity, but slower catalysis with
FT                   4alpha-carboxysterol as substrate."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         135
FT                   /note="S->T: Altered activity due to reduced affinity and
FT                   catalysis and leading to lower amount of C4-demethylated
FT                   sterols and higher quantities of 4,4-dimethylated sterol
FT                   intermediates, and a higher ratio of 4,4-dimethylsterols to
FT                   4alpha-methylsterols."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         135
FT                   /note="S->Y: Altered activity leading to an exclusive
FT                   production of C4-methylated sterols and 4alpha-carboxy-
FT                   3beta-hydroxy sterols."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         161
FT                   /note="Y->F: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         165
FT                   /note="K->I: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         320
FT                   /note="R->I: Normal activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   MUTAGEN         328
FT                   /note="R->I: Lost activity."
FT                   /evidence="ECO:0000269|PubMed:19218365"
FT   CONFLICT        49
FT                   /note="N -> D (in Ref. 6; AAM62504)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="S -> P (in Ref. 1; AAY28502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="V -> F (in Ref. 6; AAM62504)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="K -> R (in Ref. 1; AAY28502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   439 AA;  48125 MW;  C976A205FAFD87ED CRC64;
     MVMEVTETER WCVVTGGRGF AARHLVEMLV RYQMFHVRIA DLAPAIVLNP HEETGILGEA
     IRSGRVQYVS ADLRNKTQVV KGFQGAEVVF HMAAPDSSIN NHQLQYSVNV QGTTNVIDAC
     IEVGVKRLIY TSSPSVVFDG VHGTLNADES LPYPPKHNDS YSATKAEGEA LILKANGRSG
     LLTCCIRPSS IFGPGDKLMV PSLVTAARAG KSKFIIGDGS NFYDFTYVEN VVHAHVCAER
     ALASGGEVCA KAAGQAYFIT NMEPIKFWEF MSQLLEGLGY ERPSIKIPAS LMMPIAYLVE
     LAYKLLGPYG MKVPVLTPSR VRLLSCNRTF DSSKAKDRLG YSPVVPLQEG IKRTIDSFSH
     LKAQNQPKTE VTETIQWKKQ TLIAIVILIT LYHNFVATTG SSSVIITAVS KVLLVSSIFM
     FINGILPEKM KVFGSKKID
 
 
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