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CP21A_CANLU
ID   CP21A_CANLU             Reviewed;         492 AA.
AC   Q2LCM1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Steroid 21-hydroxylase;
DE            EC=1.14.14.16 {ECO:0000250|UniProtKB:P00191};
DE   AltName: Full=21-OHase;
DE   AltName: Full=Cytochrome P-450c21;
DE   AltName: Full=Cytochrome P450 21;
DE   AltName: Full=Cytochrome P450 XXI;
DE   AltName: Full=Cytochrome P450-C21;
GN   Name=CYP21;
OS   Canis lupus (Gray wolf).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Muscle;
RA   Kosowska B., Brzezinska K., Dobosz T., Moska M., Strzala T., Marszalek B.,
RA   Schmidt K.;
RT   "Phylogenetic analysis of a steroid 21-hydroxylase gene in some species of
RT   animals and a man.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids.
CC       Required for the adrenal synthesis of mineralocorticoids and
CC       glucocorticoids. {ECO:0000250|UniProtKB:P00191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 11-deoxycortisol + H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:50308, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17252, ChEBI:CHEBI:28324,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.16;
CC         Evidence={ECO:0000250|UniProtKB:P00191};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] =
CC         21-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:50304, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16973, ChEBI:CHEBI:17026, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.16;
CC         Evidence={ECO:0000250|UniProtKB:P00191};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00191};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- DOMAIN: The leucine-rich hydrophobic amino acid N-terminal region
CC       probably helps to anchor the protein to the microsomal membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; DQ336566; ABC67289.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LCM1; -.
DR   SMR; Q2LCM1; -.
DR   PRIDE; Q2LCM1; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0103069; F:17-hydroxyprogesterone 21-hydroxylase activity; IEA:RHEA.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0106309; F:progesterone 21-hydroxylase activity; IEA:RHEA.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008395; F:steroid hydroxylase activity; ISS:UniProtKB.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Lipid-binding; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Steroid-binding; Steroidogenesis.
FT   CHAIN           1..492
FT                   /note="Steroid 21-hydroxylase"
FT                   /id="PRO_0000269709"
FT   BINDING         91
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
FT   BINDING         120
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
FT   BINDING         231
FT                   /ligand="17alpha-hydroxyprogesterone"
FT                   /ligand_id="ChEBI:CHEBI:17252"
FT                   /evidence="ECO:0000250|UniProtKB:P00191"
FT   BINDING         231
FT                   /ligand="progesterone"
FT                   /ligand_id="ChEBI:CHEBI:17026"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
FT   BINDING         363
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
FT   BINDING         424
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
FT   BINDING         426
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P08686"
SQ   SEQUENCE   492 AA;  55366 MW;  8151F79FF0484A54 CRC64;
     MLLLGVLLLT VLAGARLLWG KWKLRGLHLP PLVPGCLHLL QPDLPLHLLG LTQKLGPIYR
     LRLGLQDVVV LNSKRTIEEA MVRKWVDFAG RPQTPSYKLV SLHHQDLSLG DYSLLWKAHK
     KLTRSALLLG IRSSMEPLVE QLTQEFCERM RAQAGTPVAI QKEFSLLTCA IICHLTFGDK
     EDTLVHTFHD CVQDLMRTWE HWSIQMLDII PFLRFFPNPG LWRLKRALEN RDHIVEKQLR
     QHKESMVAGQ WRDMTDYMLQ RVGRLRAEEG CGQLLEGHVH MSVVDLFIGG TETTATTLSW
     AVAFLLHHPE IQQRLQEELD RELGPGASGS RIPYRDPTRL PLLSATVAEV LRLRPVVPLA
     LPHCTTRPSS ISGYDIPEGM VVIPNLQGAH LDETVWERPQ EFRPDRFLVP GASPRVLAFG
     CGARVCLGEP LARLELLVVL AQLLRAFTLM PAAGTLPSLR PRARCGVNLS MQPFQVQLQP
     RGAGVLGRGQ HP
 
 
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