ID   ERG25_RAT               Reviewed;         293 AA.
AC   O35532;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=C-4 methylsterol oxidase;
DE            EC=1.14.13.72;
DE   AltName: Full=Methylsterol monooxygenase;
DE   AltName: Full=Neuropep 1;
DE   AltName: Full=RANP-1;
GN   Name=Sc4mol;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=97428164; PubMed=9284352; DOI=10.1016/S0306-4522(97)00112-7;
RA   Uwabe K., Gahara Y., Yamada H., Miyake T., Kitamura T.;
RT   "Identification and characterization of a novel gene (neurorep 1)
RT   expressed in nerve cells and up-regulated after axotomy.";
RL   Neuroscience 80:501-509(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol +
CC       NAD(P)H + O(2) = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-
CC       cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-
CC       cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-
CC       methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2
CC       H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-
CC       7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4-
CC       beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+)
CC       + H(2)O.
CC   -!- COFACTOR: Iron (Probable).
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 3/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (Probable).
CC   -!- DOMAIN: The histidine box domains may contain the active site
CC       and/or be involved in metal ion binding.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family.
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DR   EMBL; D50559; BAA23329.1; -; mRNA.
DR   EMBL; BC063155; AAH63155.1; -; mRNA.
DR   IPI; IPI00210465; -.
DR   RefSeq; NP_543162.1; -.
DR   UniGene; Rn.7167; -.
DR   PRIDE; O35532; -.
DR   Ensembl; ENSRNOG00000032297; Rattus norvegicus.
DR   GeneID; 140910; -.
DR   KEGG; rno:140910; -.
DR   RGD; 620281; Sc4mol.
DR   HOVERGEN; O35532; -.
DR   OMA; O35532; NPLHLIP.
DR   BRENDA; 1.14.13.72; 248.
DR   NextBio; 620749; -.
DR   ArrayExpress; O35532; -.
DR   GermOnline; ENSRNOG00000032297; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000254; F:C-4 methylsterol oxidase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD;
KW   Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis;
KW   Transmembrane.
FT   CHAIN         1    293       C-4 methylsterol oxidase.
FT                                /FTId=PRO_0000117036.
FT   TRANSMEM     55     75       Potential.
FT   TRANSMEM    100    120       Potential.
FT   TRANSMEM    199    219       Potential.
FT   MOTIF       157    161       Histidine box-1.
FT   MOTIF       170    174       Histidine box-2.
FT   MOTIF       249    255       Histidine box-3.
SQ   SEQUENCE   293 AA;  34964 MW;  FEE8C22FDC5F38D7 CRC64;
     MAMNKSVGLF SSASLAVDYV DSLLPENPLQ EPFKNAWVYM LDNYTKFQIA TWGSLIVHET
     IYFLFSLPGF LFQFIPFMRK YKIQKDKPET FEGQWKCLKG ILFNHFFIQL PLICGTYYFT
     EFFNIPYDWE RMPRWYFTLA RCLGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF
     GIEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTMR LLETIDVHSG YDIPLNPLNY
     IPFYTGARHH DFHHMNFIGN YASTFTWWDR IFGTDVQYHA YTEKMKKLGK KSE
//