P05108 (CP11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CYP11A1
Synonyms:	CYP11A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.
Catalytic activity	Cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O.
Cofactor	Heme group.
Pathway	Lipid metabolism; C21-steroid hormone metabolism.
Subunit structure	Interacts with FDX1/adrenodoxin.
Subcellular location	Mitochondrion membrane.
Induction	By 8-bromo cyclic AMP. Ref.8
Involvement in disease	Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR) [MIM:613743]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Steroid metabolism Steroidogenesis Sterol metabolism
Cellular component	Membrane Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	C21-steroid hormone biosynthetic process Inferred from direct assay Ref.13Ref.16. Source: UniProtKB Leydig cell differentiation Inferred from electronic annotation. Source: Compara Schwann cell differentiation Inferred from electronic annotation. Source: Compara biphenyl metabolic process Inferred from electronic annotation. Source: Compara cellular response to antibiotic Inferred from electronic annotation. Source: Compara cellular response to cAMP Inferred from electronic annotation. Source: Compara cellular response to cadmium ion Inferred from electronic annotation. Source: Compara cellular response to fibroblast growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara cerebellum development Inferred from electronic annotation. Source: Compara cholesterol metabolic process Inferred from mutant phenotype Ref.16. Source: UniProtKB dibenzo-p-dioxin metabolic process Inferred from electronic annotation. Source: Compara estrogen biosynthetic process Inferred from electronic annotation. Source: Compara fractalkine metabolic process Inferred from electronic annotation. Source: Compara granulosa cell differentiation Inferred from electronic annotation. Source: Compara hippocampus development Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara mating behavior Inferred from electronic annotation. Source: Compara phenol-containing compound metabolic process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara progesterone biosynthetic process Inferred from electronic annotation. Source: Compara response to L-ascorbic acid Inferred from electronic annotation. Source: Compara response to acid Inferred from electronic annotation. Source: Compara response to alkaloid Inferred from electronic annotation. Source: Compara response to corticosterone stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to fungicide Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to genistein Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to insecticide Inferred from electronic annotation. Source: Compara response to salt stress Inferred from electronic annotation. Source: Compara response to vitamin E Inferred from electronic annotation. Source: Compara testosterone biosynthetic process Inferred from electronic annotation. Source: Compara vitamin D metabolic process Inferred from sequence or structural similarity. Source: UniProtKB xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial crista Inferred from electronic annotation. Source: Compara mitochondrial matrix Traceable author statement. Source: Reactome perikaryon Inferred from electronic annotation. Source: Compara
Molecular_function	cholesterol binding Inferred from electronic annotation. Source: Compara cholesterol monooxygenase (side-chain-cleaving) activity Inferred from direct assay Ref.13Ref.16. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P05108-1)

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.

Isoform 2 (identifier: P05108-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

39

Mitochondrion

Chain

40 – 521

482

Cholesterol side-chain cleavage enzyme, mitochondrial

PRO_0000003585

Sites

Metal binding

462

1

Iron (heme axial ligand)

Natural variations

Alternative sequence

1 – 158

158

Missing in isoform 2.

VSP_045695

Natural variant

141

1

L → W in AICSR; reduced activity. Ref.16

VAR_065241

Natural variant

189

1

A → V in AICSR; no loss of activity. Ref.14

VAR_016949

Natural variant

222

1

L → P in AICSR; markedly reduced activity. Ref.17

VAR_065242

Natural variant

271

1

D → DGD in AICSR; complete loss of activity.

VAR_016950

Natural variant

314

1

E → K. Ref.11
Corresponds to variant rs6161 [ dbSNP | Ensembl ].

VAR_013944

Natural variant

353

1

R → W in AICSR; loss of activity. Ref.14

VAR_016951

Natural variant

359

1

A → V in AICSR; markedly reduced activity. Ref.15

VAR_065243

Natural variant

415

1

V → E in AICSR; complete loss of activity. Ref.16

VAR_065244

Experimental info

Sequence conflict

16

1

C → Y in AAA52162. Ref.1

Sequence conflict

274

1

F → L in CAA28965. Ref.2

Sequence conflict

283

1

N → H in AAA36404. Ref.9

Sequence conflict

301

1

I → M in AAA52162. Ref.1

Sequence conflict

301

1

I → M in AAA36404. Ref.9

Sequence conflict

505

1

K → E in BAG51810. Ref.3

Secondary structure

1

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521

Helix Strand Turn

Details...

Helix

48 – 50

3

Helix

58 – 68

11

Helix

71 – 73

3

Helix

74 – 85

12

Beta strand

87 – 93

7

Beta strand

96 – 101

6

Helix

104 – 112

9

Helix

124 – 132

9

Helix

139 – 141

3

Helix

144 – 158

15

Helix

161 – 164

4

Helix

167 – 189

23

Beta strand

190 – 196

7

Helix

199 – 215

17

Beta strand

223 – 225

3

Helix

228 – 244

17

Helix

245 – 247

3

Helix

252 – 258

7

Helix

260 – 291

32

Helix

301 – 307

7

Helix

313 – 328

16

Helix

330 – 344

15

Helix

346 – 362

17

Turn

363 – 365

3

Helix

367 – 370

4

Helix

375 – 387

13

Beta strand

390 – 397

8

Beta strand

402 – 404

3

Beta strand

407 – 409

3

Beta strand

414 – 418

5

Helix

419 – 423

5

Turn

426 – 428

3

Beta strand

429 – 431

3

Helix

437 – 440

4

Turn

449 – 451

3

Helix

458 – 460

3

Helix

465 – 482

18

Beta strand

483 – 486

4

Beta strand

495 – 505

11

Beta strand

509 – 513

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: AB0501E7A5665D8B	FASTA	521	60,102
	10 20 30 40 50 60 MLAKGLPPRS VLVKGCQTFL SAPREGLGRL RVPTGEGAGI STRSPRPFNE IPSPGDNGWL 70 80 90 100 110 120 NLYHFWRETG THKVHLHHVQ NFQKYGPIYR EKLGNVESVY VIDPEDVALL FKSEGPNPER 130 140 150 160 170 180 FLIPPWVAYH QYYQRPIGVL LKKSAAWKKD RVALNQEVMA PEATKNFLPL LDAVSRDFVS 190 200 210 220 230 240 VLHRRIKKAG SGNYSGDISD DLFRFAFESI TNVIFGERQG MLEEVVNPEA QRFIDAIYQM 250 260 270 280 290 300 FHTSVPMLNL PPDLFRLFRT KTWKDHVAAW DVIFSKADIY TQNFYWELRQ KGSVHHDYRG 310 320 330 340 350 360 ILYRLLGDSK MSFEDIKANV TEMLAGGVDT TSMTLQWHLY EMARNLKVQD MLRAEVLAAR 370 380 390 400 410 420 HQAQGDMATM LQLVPLLKAS IKETLRLHPI SVTLQRYLVN DLVLRDYMIP AKTLVQVAIY 430 440 450 460 470 480 ALGREPTFFF DPENFDPTRW LSKDKNITYF RNLGFGWGVR QCLGRRIAEL EMTIFLINML 490 500 510 520 ENFRVEIQHL SDVGTTFNLI LMPEKPISFT FWPFNQEATQ Q
	Isoform 2 [UniParc]. Checksum: 8CA4719AAC24EF8B	FASTA	363	42,152
	10 20 30 40 50 60 MAPEATKNFL PLLDAVSRDF VSVLHRRIKK AGSGNYSGDI SDDLFRFAFE SITNVIFGER 70 80 90 100 110 120 QGMLEEVVNP EAQRFIDAIY QMFHTSVPML NLPPDLFRLF RTKTWKDHVA AWDVIFSKAD 130 140 150 160 170 180 IYTQNFYWEL RQKGSVHHDY RGILYRLLGD SKMSFEDIKA NVTEMLAGGV DTTSMTLQWH 190 200 210 220 230 240 LYEMARNLKV QDMLRAEVLA ARHQAQGDMA TMLQLVPLLK ASIKETLRLH PISVTLQRYL 250 260 270 280 290 300 VNDLVLRDYM IPAKTLVQVA IYALGREPTF FFDPENFDPT RWLSKDKNIT YFRNLGFGWG 310 320 330 340 350 360 VRQCLGRRIA ELEMTIFLIN MLENFRVEIQ HLSDVGTTFN LILMPEKPIS FTFWPFNQEA TQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LYS-314.
[12]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00295771.

PIR

A25922.

RefSeq

NP_000772.2. NM_000781.2.
NP_001093243.1. NM_001099773.1.

UniGene

Hs.303980.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3N9Y	X-ray	2.10	A/B	41-521	[»]
3N9Z	X-ray	2.17	A/B	41-521	[»]
3NA0	X-ray	2.50	A/B	44-514	[»]
3NA1	X-ray	2.25	A/B	41-521	[»]

ProteinModelPortal

P05108.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1200919.

STRING

9606.ENSP00000268053.

PTM databases

PhosphoSite

P05108.

Polymorphism databases

DMDM

143811381.

Proteomic databases

PaxDb

P05108.

PRIDE

P05108.

Protocols and materials databases

DNASU

1583.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268053; ENSP00000268053; ENSG00000140459.
ENST00000358632; ENSP00000351455; ENSG00000140459.
ENST00000419019; ENSP00000405488; ENSG00000140459.

GeneID

1583.

KEGG

hsa:1583.

UCSC

uc002axs.2. human.

Organism-specific databases

CTD

1583.

GeneCards

GC15M074630.

HGNC

HGNC:2590. CYP11A1.

HPA

HPA016436.

MIM

118485. gene.
613743. phenotype.

neXtProt

NX_P05108.

Orphanet

168558. 46,XY disorder of sex development - adrenal insufficiency.
289548. Inherited isolated adrenal insufficiency.

PharmGKB

PA27089.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000013161.

HOVERGEN

HBG051098.

InParanoid

P05108.

KO

K00498.

OMA

RDYMIPA.

OrthoDB

EOG4GXFMF.

Enzyme and pathway databases

BioCyc

MetaCyc:HS06719-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_15493. Steroid hormones.

SABIO-RK

P05108.

UniPathway

UPA00229.

Gene expression databases

ArrayExpress

P05108.

Bgee

P05108.

CleanEx

HS_CYP11A1.

Genevestigator

P05108.

GermOnline

ENSG00000140459. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL2033.

ChiTaRS

CYP11A1. human.

DrugBank

DB00357. Aminoglutethimide.
DB00169. Cholecalciferol.
DB00501. Cimetidine.
DB00257. Clotrimazole.
DB01396. Digitoxin.
DB00390. Digoxin.
DB00603. Medroxyprogesterone.
DB01092. Ouabain.
DB00396. Progesterone.
DB00624. Testosterone.
DB01108. Trilostane.

EvolutionaryTrace

P05108.

GenomeRNAi

1583.

NextBio

35469259.

SOURCE

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Entry information

Entry name

CP11A_HUMAN

Accession

Primary (citable) accession number: P05108
Secondary accession number(s): A8K8D5 , B3KPU8, G3XAD7, Q15081, Q16805, Q8N1A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.