ID G1PWA2_MYOLU Unreviewed; 492 AA.
AC G1PWA2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Cytochrome P450 family 7 subfamily B member 1 {ECO:0000313|Ensembl:ENSMLUP00000015664.2};
GN Name=CYP7B1 {ECO:0000313|Ensembl:ENSMLUP00000015664.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000015664.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000015664.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000015664.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR000047, ECO:0000256|PIRSR:PIRSR000047-1};
CC -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004860}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR000047}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|PIRNR:PIRNR000047}.
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DR EMBL; AAPE02021746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PWA2; -.
DR STRING; 59463.ENSMLUP00000015664; -.
DR Ensembl; ENSMLUT00000017182.2; ENSMLUP00000015664.2; ENSMLUG00000017179.2.
DR eggNOG; KOG0684; Eukaryota.
DR GeneTree; ENSGT00940000153141; -.
DR HOGENOM; CLU_018012_1_2_1; -.
DR InParanoid; G1PWA2; -.
DR OMA; WSEVVQM; -.
DR TreeFam; TF105090; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008396; F:oxysterol 7-alpha-hydroxylase activity; IEA:Ensembl.
DR GO; GO:0035754; P:B cell chemotaxis; IEA:Ensembl.
DR GO; GO:0006699; P:bile acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF0; CYTOCHROME P450 7B1; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000047};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000047};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000047};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Membrane {ECO:0000256|PIRNR:PIRNR000047};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000047};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Signal {ECO:0000256|SAM:SignalP};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..492
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003419142"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT BINDING 434
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000047-1"
SQ SEQUENCE 492 AA; 57165 MW; 7D473F464D266874 CRC64;
KIYKVMTWCL IVLSCCCQNK LLFFSYRRPG EPPLLKGWLP YFGLALKLQK DPIGFMRTLQ
NQHGDTFTLL LGGKYITFIL DPYQYQSVMK NQKLSFRMFS KNILKKAFAI QKLMTDDELN
NELHDCYKLL QGKSLDLLME NMTQNLQQVF EPKLFKTTNW DMAYLLTFCS SVIFEATFAT
IYGKSVAGDR KEFITELKDD FFKFDAKFIY LLSDIPIELL GDAKSIQKKL IKHLTSENLA
NIQGWSEVVQ MRQDILEKYY TLKDIEIGAH HLGFLWASVA NTIPTMFWTI YYLLRHPEAM
AVLRDEIDHL LQSTGQKQGS GFSIYITREQ LDSLVYLESA ILEALRLCSF SSIIRFVQED
LTLPSETGDY LIRKGDLVAI FPPLMHHDPE IFEAPEEYRF DRFVENGKKK TNFFKGGKRL
KHYILPFGMG ASKCPGRFLA INEIKQLLVV LLTNFDLEIM DDKPVQLDYG RFLIGIQYPD
SDVLFRYKVK SQ
//
