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Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.1 Publication

Catalytic activityi

Cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O.1 Publication

Cofactori

heme1 Publication

Pathway:iC21-steroid hormone metabolism

This protein is involved in the pathway C21-steroid hormone metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway C21-steroid hormone metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi462 – 4621Iron (heme axial ligand)

GO - Molecular functioni

  • cholesterol binding Source: Ensembl
  • cholesterol monooxygenase (side-chain-cleaving) activity Source: UniProtKB
  • heme binding Source: UniProtKB
  • iron ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06719-MONOMER.
BRENDAi1.14.15.6. 2681.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).
SABIO-RKP05108.
UniPathwayiUPA00229.

Names & Taxonomyi

Protein namesi
Recommended name:
Cholesterol side-chain cleavage enzyme, mitochondrial (EC:1.14.15.6)
Alternative name(s):
CYPXIA1
Cholesterol desmolase
Cytochrome P450 11A1
Cytochrome P450(scc)
Gene namesi
Name:CYP11A1
Synonyms:CYP11A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:2590. CYP11A1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare disorder that can present as acute adrenal insufficiency in infancy or childhood. ACTH and plasma renin activity are elevated and adrenal steroids are inappropriately low or absent; the 46,XY patients have female external genitalia, sometimes with clitoromegaly. The phenotypic spectrum ranges from prematurity, complete underandrogenization, and severe early-onset adrenal failure to term birth with clitoromegaly and later-onset adrenal failure. Patients with congenital adrenal insufficiency do not manifest the massive adrenal enlargement typical of congenital lipoid adrenal hyperplasia.

See also OMIM:613743
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411L → W in AICSR; reduced activity. 1 Publication
VAR_065241
Natural varianti189 – 1891A → V in AICSR; no loss of activity. 1 Publication
VAR_016949
Natural varianti222 – 2221L → P in AICSR; markedly reduced activity. 1 Publication
VAR_065242
Natural varianti271 – 2711D → DGD in AICSR; complete loss of activity. 1 Publication
VAR_016950
Natural varianti353 – 3531R → W in AICSR; loss of activity. 1 Publication
VAR_016951
Natural varianti359 – 3591A → V in AICSR; markedly reduced activity. 1 Publication
VAR_065243
Natural varianti415 – 4151V → E in AICSR; complete loss of activity. 1 Publication
VAR_065244

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613743. phenotype.
Orphaneti168558. 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
289548. Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
PharmGKBiPA27089.

Chemistry

DrugBankiDB00357. Aminoglutethimide.
DB00169. Cholecalciferol.
DB00882. Clomifene.
DB00257. Clotrimazole.
DB01234. Dexamethasone.
DB01396. Digitoxin.
DB00390. Digoxin.
DB00917. Dinoprostone.
DB01437. Glutethimide.
DB01026. Ketoconazole.
DB00338. Omeprazole.
DB01232. Saquinavir.
DB00857. Terbinafine.
DB00624. Testosterone.

Polymorphism and mutation databases

BioMutaiCYP11A1.
DMDMi143811381.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionAdd
BLAST
Chaini40 – 521482Cholesterol side-chain cleavage enzyme, mitochondrialPRO_0000003585Add
BLAST

Proteomic databases

PaxDbiP05108.
PRIDEiP05108.

PTM databases

PhosphoSiteiP05108.

Expressioni

Inductioni

By 8-bromo cyclic AMP.1 Publication

Gene expression databases

BgeeiP05108.
CleanExiHS_CYP11A1.
ExpressionAtlasiP05108. baseline and differential.
GenevisibleiP05108. HS.

Organism-specific databases

HPAiHPA016436.

Interactioni

Subunit structurei

Interacts with FDX1/adrenodoxin.1 Publication

Protein-protein interaction databases

BioGridi107955. 4 interactions.
IntActiP05108. 4 interactions.
MINTiMINT-1200919.
STRINGi9606.ENSP00000268053.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 503Combined sources
Helixi58 – 6811Combined sources
Helixi71 – 733Combined sources
Helixi74 – 8512Combined sources
Beta strandi87 – 937Combined sources
Beta strandi96 – 1016Combined sources
Helixi104 – 1129Combined sources
Helixi124 – 1329Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 15815Combined sources
Helixi161 – 1644Combined sources
Helixi167 – 18923Combined sources
Beta strandi190 – 1967Combined sources
Helixi199 – 21517Combined sources
Beta strandi223 – 2253Combined sources
Helixi228 – 24417Combined sources
Helixi245 – 2473Combined sources
Helixi252 – 2587Combined sources
Helixi260 – 29132Combined sources
Helixi301 – 3077Combined sources
Helixi313 – 32816Combined sources
Helixi330 – 34415Combined sources
Helixi346 – 36217Combined sources
Turni363 – 3653Combined sources
Helixi367 – 3704Combined sources
Helixi375 – 38713Combined sources
Beta strandi390 – 3978Combined sources
Beta strandi402 – 4043Combined sources
Beta strandi407 – 4093Combined sources
Beta strandi414 – 4185Combined sources
Helixi419 – 4235Combined sources
Turni426 – 4283Combined sources
Beta strandi429 – 4313Combined sources
Helixi437 – 4404Combined sources
Turni449 – 4513Combined sources
Helixi458 – 4603Combined sources
Helixi465 – 48218Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi495 – 50511Combined sources
Beta strandi509 – 5135Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10A/B41-521[»]
3N9ZX-ray2.17A/B41-521[»]
3NA0X-ray2.50A/B44-514[»]
3NA1X-ray2.25A/B41-521[»]
ProteinModelPortaliP05108.
SMRiP05108. Positions 44-514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05108.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP05108.
KOiK00498.
OMAiAIYQMFH.
OrthoDBiEOG7MKW5S.
PhylomeDBiP05108.
TreeFamiTF105094.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05108-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLAKGLPPRS VLVKGCQTFL SAPREGLGRL RVPTGEGAGI STRSPRPFNE
60 70 80 90 100
IPSPGDNGWL NLYHFWRETG THKVHLHHVQ NFQKYGPIYR EKLGNVESVY
110 120 130 140 150
VIDPEDVALL FKSEGPNPER FLIPPWVAYH QYYQRPIGVL LKKSAAWKKD
160 170 180 190 200
RVALNQEVMA PEATKNFLPL LDAVSRDFVS VLHRRIKKAG SGNYSGDISD
210 220 230 240 250
DLFRFAFESI TNVIFGERQG MLEEVVNPEA QRFIDAIYQM FHTSVPMLNL
260 270 280 290 300
PPDLFRLFRT KTWKDHVAAW DVIFSKADIY TQNFYWELRQ KGSVHHDYRG
310 320 330 340 350
ILYRLLGDSK MSFEDIKANV TEMLAGGVDT TSMTLQWHLY EMARNLKVQD
360 370 380 390 400
MLRAEVLAAR HQAQGDMATM LQLVPLLKAS IKETLRLHPI SVTLQRYLVN
410 420 430 440 450
DLVLRDYMIP AKTLVQVAIY ALGREPTFFF DPENFDPTRW LSKDKNITYF
460 470 480 490 500
RNLGFGWGVR QCLGRRIAEL EMTIFLINML ENFRVEIQHL SDVGTTFNLI
510 520
LMPEKPISFT FWPFNQEATQ Q
Length:521
Mass (Da):60,102
Last modified:April 3, 2007 - v2
Checksum:iAB0501E7A5665D8B
GO
Isoform 2 (identifier: P05108-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.

Note: No experimental confirmation available.
Show »
Length:363
Mass (Da):42,152
Checksum:i8CA4719AAC24EF8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → Y in AAA52162 (PubMed:3024157).Curated
Sequence conflicti274 – 2741F → L in CAA28965 (PubMed:3038854).Curated
Sequence conflicti283 – 2831N → H in AAA36404 (PubMed:2419119).Curated
Sequence conflicti301 – 3011I → M in AAA52162 (PubMed:3024157).Curated
Sequence conflicti301 – 3011I → M in AAA36404 (PubMed:2419119).Curated
Sequence conflicti505 – 5051K → E in BAG51810 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411L → W in AICSR; reduced activity. 1 Publication
VAR_065241
Natural varianti189 – 1891A → V in AICSR; no loss of activity. 1 Publication
VAR_016949
Natural varianti222 – 2221L → P in AICSR; markedly reduced activity. 1 Publication
VAR_065242
Natural varianti271 – 2711D → DGD in AICSR; complete loss of activity. 1 Publication
VAR_016950
Natural varianti314 – 3141E → K.1 Publication
Corresponds to variant rs6161 [ dbSNP | Ensembl ].
VAR_013944
Natural varianti353 – 3531R → W in AICSR; loss of activity. 1 Publication
VAR_016951
Natural varianti359 – 3591A → V in AICSR; markedly reduced activity. 1 Publication
VAR_065243
Natural varianti415 – 4151V → E in AICSR; complete loss of activity. 1 Publication
VAR_065244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 2. 1 PublicationVSP_045695Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14565 mRNA. Translation: AAA52162.1.
X05367
, X05368, X05369, X05370, X05371, X05372, X05373, X05374 Genomic DNA. Translation: CAA28965.1.
AK056794 mRNA. Translation: BAG51810.1.
AK292300 mRNA. Translation: BAF84989.1.
AC090826 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99341.1.
CH471136 Genomic DNA. Translation: EAW99342.1.
BC032329 mRNA. Translation: AAH32329.1.
X14257 Genomic DNA. Translation: CAA32471.1.
M28253 mRNA. Translation: AAA36404.1.
CCDSiCCDS32291.1. [P05108-1]
CCDS45303.1. [P05108-2]
PIRiA25922.
RefSeqiNP_000772.2. NM_000781.2. [P05108-1]
NP_001093243.1. NM_001099773.1. [P05108-2]
UniGeneiHs.303980.

Genome annotation databases

EnsembliENST00000268053; ENSP00000268053; ENSG00000140459.
ENST00000358632; ENSP00000351455; ENSG00000140459. [P05108-2]
GeneIDi1583.
KEGGihsa:1583.
UCSCiuc002axs.2. human. [P05108-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14565 mRNA. Translation: AAA52162.1.
X05367
, X05368, X05369, X05370, X05371, X05372, X05373, X05374 Genomic DNA. Translation: CAA28965.1.
AK056794 mRNA. Translation: BAG51810.1.
AK292300 mRNA. Translation: BAF84989.1.
AC090826 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99341.1.
CH471136 Genomic DNA. Translation: EAW99342.1.
BC032329 mRNA. Translation: AAH32329.1.
X14257 Genomic DNA. Translation: CAA32471.1.
M28253 mRNA. Translation: AAA36404.1.
CCDSiCCDS32291.1. [P05108-1]
CCDS45303.1. [P05108-2]
PIRiA25922.
RefSeqiNP_000772.2. NM_000781.2. [P05108-1]
NP_001093243.1. NM_001099773.1. [P05108-2]
UniGeneiHs.303980.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N9YX-ray2.10A/B41-521[»]
3N9ZX-ray2.17A/B41-521[»]
3NA0X-ray2.50A/B44-514[»]
3NA1X-ray2.25A/B41-521[»]
ProteinModelPortaliP05108.
SMRiP05108. Positions 44-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107955. 4 interactions.
IntActiP05108. 4 interactions.
MINTiMINT-1200919.
STRINGi9606.ENSP00000268053.

Chemistry

BindingDBiP05108.
ChEMBLiCHEMBL2033.
DrugBankiDB00357. Aminoglutethimide.
DB00169. Cholecalciferol.
DB00882. Clomifene.
DB00257. Clotrimazole.
DB01234. Dexamethasone.
DB01396. Digitoxin.
DB00390. Digoxin.
DB00917. Dinoprostone.
DB01437. Glutethimide.
DB01026. Ketoconazole.
DB00338. Omeprazole.
DB01232. Saquinavir.
DB00857. Terbinafine.
DB00624. Testosterone.
GuidetoPHARMACOLOGYi1358.

PTM databases

PhosphoSiteiP05108.

Polymorphism and mutation databases

BioMutaiCYP11A1.
DMDMi143811381.

Proteomic databases

PaxDbiP05108.
PRIDEiP05108.

Protocols and materials databases

DNASUi1583.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268053; ENSP00000268053; ENSG00000140459.
ENST00000358632; ENSP00000351455; ENSG00000140459. [P05108-2]
GeneIDi1583.
KEGGihsa:1583.
UCSCiuc002axs.2. human. [P05108-1]

Organism-specific databases

CTDi1583.
GeneCardsiGC15M074630.
HGNCiHGNC:2590. CYP11A1.
HPAiHPA016436.
MIMi118485. gene.
613743. phenotype.
neXtProtiNX_P05108.
Orphaneti168558. 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
289548. Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
PharmGKBiPA27089.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000119243.
HOGENOMiHOG000013161.
HOVERGENiHBG051098.
InParanoidiP05108.
KOiK00498.
OMAiAIYQMFH.
OrthoDBiEOG7MKW5S.
PhylomeDBiP05108.
TreeFamiTF105094.

Enzyme and pathway databases

UniPathwayiUPA00229.
BioCyciMetaCyc:HS06719-MONOMER.
BRENDAi1.14.15.6. 2681.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
REACT_13812. Endogenous sterols.
REACT_268767. Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).
SABIO-RKP05108.

Miscellaneous databases

ChiTaRSiCYP11A1. human.
EvolutionaryTraceiP05108.
GeneWikiiCholesterol_side-chain_cleavage_enzyme.
GenomeRNAii1583.
NextBioi35469259.
PROiP05108.
SOURCEiSearch...

Gene expression databases

BgeeiP05108.
CleanExiHS_CYP11A1.
ExpressionAtlasiP05108. baseline and differential.
GenevisibleiP05108. HS.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta."
    Chung B.-C., Matteson K.J., Voutilainen R., Mohandas T.K., Miller W.L.
    Proc. Natl. Acad. Sci. U.S.A. 83:8962-8966(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Gene structure of human cytochrome P-450(SCC), cholesterol desmolase."
    Morohashi K., Sogawa K., Omura T., Fujii-Kuriyama Y.
    J. Biochem. 101:879-887(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Testis.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. Chung B.-C.
    Submitted (JAN-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
  8. "Regulated expression of cytochrome P-450scc (cholesterol-side-chain cleavage enzyme) in cultured cell lines detected by antibody against bacterially expressed human protein."
    Hu M.C., Guo I.C., Lin J.H., Chung B.-C.
    Biochem. J. 274:813-817(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-54, INDUCTION.
    Tissue: Choriocarcinoma.
  9. "Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency causing congenital lipoid adrenal hyperplasia using bovine-sequence P450scc oligodeoxyribonucleotide probes."
    Matteson K.J., Chung B.-C., Urdea M.S., Miller W.L.
    Endocrinology 118:1296-1305(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 283-521 (ISOFORM 1).
  10. "Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system."
    Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S., Park H.W.
    Proc. Natl. Acad. Sci. U.S.A. 108:10139-10143(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 41-521 IN COMPLEXES WITH FDX1; HEME AND CHOLESTEROL, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, INTERACTION WITH FDX1.
  11. Cited for: VARIANT LYS-314.
  12. "Heterozygous mutation in the cholesterol side chain cleavage enzyme (P450scc) gene in a patient with 46,XY sex reversal and adrenal insufficiency."
    Tajima T., Fujieda K., Kouda N., Nakae J., Miller W.L.
    J. Clin. Endocrinol. Metab. 86:3820-3825(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR GLY-ASP-271 INS.
  13. "Compound heterozygous mutations in the cholesterol side-chain cleavage enzyme gene (CYP11A) cause congenital adrenal insufficiency in humans."
    Katsumata N., Ohtake M., Hojo T., Ogawa E., Hara T., Sato N., Tanaka T.
    J. Clin. Endocrinol. Metab. 87:3808-3813(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AICSR VAL-189 AND TRP-353.
  14. "Homozygous mutation of P450 side-chain cleavage enzyme gene (CYP11A1) in 46, XY patient with adrenal insufficiency, complete sex reversal, and agenesis of corpus callosum."
    al Kandari H., Katsumata N., Alexander S., Rasoul M.A.
    J. Clin. Endocrinol. Metab. 91:2821-2826(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR VAL-359, CHARACTERIZATION OF VARIANT AICSR VAL-359.
  15. "Severe combined adrenal and gonadal deficiency caused by novel mutations in the cholesterol side chain cleavage enzyme, P450scc."
    Kim C.J., Lin L., Huang N., Quigley C.A., Avruskin T.W., Achermann J.C., Miller W.L.
    J. Clin. Endocrinol. Metab. 93:696-702(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AICSR TRP-141 AND GLU-415, CHARACTERIZATION OF VARIANTS AICSR TRP-141 AND GLU-415.
  16. "A novel homozygous mutation in CYP11A1 gene is associated with late-onset adrenal insufficiency and hypospadias in a 46,XY patient."
    Rubtsov P., Karmanov M., Sverdlova P., Spirin P., Tiulpakov A.
    J. Clin. Endocrinol. Metab. 94:936-939(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AICSR PRO-222, CHARACTERIZATION OF VARIANT AICSR PRO-222.

Entry informationi

Entry nameiCP11A_HUMAN
AccessioniPrimary (citable) accession number: P05108
Secondary accession number(s): A8K8D5
, B3KPU8, G3XAD7, Q15081, Q16805, Q8N1A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 3, 2007
Last modified: July 22, 2015
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.