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P05108

- CP11A_HUMAN

UniProt

P05108 - CP11A_HUMAN

Protein

Cholesterol side-chain cleavage enzyme, mitochondrial

Gene

CYP11A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Heme group.1 Publication

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. cholesterol binding Source: Ensembl
    2. cholesterol monooxygenase (side-chain-cleaving) activity Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. iron ion binding Source: InterPro

    GO - Biological processi

    1. biphenyl metabolic process Source: Ensembl
    2. C21-steroid hormone biosynthetic process Source: UniProtKB
    3. cellular response to antibiotic Source: Ensembl
    4. cellular response to cadmium ion Source: Ensembl
    5. cellular response to cAMP Source: Ensembl
    6. cellular response to fibroblast growth factor stimulus Source: Ensembl
    7. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
    8. cellular response to interleukin-1 Source: Ensembl
    9. cellular response to lipopolysaccharide Source: Ensembl
    10. cellular response to peptide hormone stimulus Source: Ensembl
    11. cellular response to transforming growth factor beta stimulus Source: Ensembl
    12. cellular response to tumor necrosis factor Source: Ensembl
    13. cerebellum development Source: Ensembl
    14. cholesterol metabolic process Source: UniProtKB
    15. dibenzo-p-dioxin metabolic process Source: Ensembl
    16. estrogen biosynthetic process Source: Ensembl
    17. fractalkine metabolic process Source: Ensembl
    18. granulosa cell differentiation Source: Ensembl
    19. hippocampus development Source: Ensembl
    20. Leydig cell differentiation Source: Ensembl
    21. maternal process involved in female pregnancy Source: Ensembl
    22. mating behavior Source: Ensembl
    23. phenol-containing compound metabolic process Source: Ensembl
    24. phthalate metabolic process Source: Ensembl
    25. progesterone biosynthetic process Source: Ensembl
    26. response to alkaloid Source: Ensembl
    27. response to corticosterone Source: Ensembl
    28. response to drug Source: Ensembl
    29. response to fungicide Source: Ensembl
    30. response to gamma radiation Source: Ensembl
    31. response to genistein Source: Ensembl
    32. response to hydrogen peroxide Source: Ensembl
    33. response to insecticide Source: Ensembl
    34. response to L-ascorbic acid Source: Ensembl
    35. response to salt stress Source: Ensembl
    36. response to vitamin E Source: Ensembl
    37. Schwann cell differentiation Source: Ensembl
    38. small molecule metabolic process Source: Reactome
    39. steroid metabolic process Source: Reactome
    40. sterol metabolic process Source: Reactome
    41. testosterone biosynthetic process Source: Ensembl
    42. vitamin D metabolic process Source: UniProtKB
    43. xenobiotic metabolic process Source: Reactome

    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.
    ReactomeiREACT_11038. Pregnenolone biosynthesis.
    REACT_13812. Endogenous sterols.
    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: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2590. CYP11A1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial crista Source: Ensembl
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProtKB
    4. perikaryon Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP05108.
    BgeeiP05108.
    CleanExiHS_CYP11A1.
    GenevestigatoriP05108.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000013161.
    HOVERGENiHBG051098.
    InParanoidiP05108.
    KOiK00498.
    OMAiYQRPIGV.
    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. Align

    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

    MLAKGLPPRS VLVKGCQTFL SAPREGLGRL RVPTGEGAGI STRSPRPFNE    50
    IPSPGDNGWL NLYHFWRETG THKVHLHHVQ NFQKYGPIYR EKLGNVESVY 100
    VIDPEDVALL FKSEGPNPER FLIPPWVAYH QYYQRPIGVL LKKSAAWKKD 150
    RVALNQEVMA PEATKNFLPL LDAVSRDFVS VLHRRIKKAG SGNYSGDISD 200
    DLFRFAFESI TNVIFGERQG MLEEVVNPEA QRFIDAIYQM FHTSVPMLNL 250
    PPDLFRLFRT KTWKDHVAAW DVIFSKADIY TQNFYWELRQ KGSVHHDYRG 300
    ILYRLLGDSK MSFEDIKANV TEMLAGGVDT TSMTLQWHLY EMARNLKVQD 350
    MLRAEVLAAR HQAQGDMATM LQLVPLLKAS IKETLRLHPI SVTLQRYLVN 400
    DLVLRDYMIP AKTLVQVAIY ALGREPTFFF DPENFDPTRW LSKDKNITYF 450
    RNLGFGWGVR QCLGRRIAEL EMTIFLINML ENFRVEIQHL SDVGTTFNLI 500
    LMPEKPISFT FWPFNQEATQ Q 521
    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:
    EMBL
    GenBank
    DDBJ
    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. [P05108-1]
    ENST00000358632; ENSP00000351455; ENSG00000140459. [P05108-2]
    GeneIDi1583.
    KEGGihsa:1583.
    UCSCiuc002axs.2. human. [P05108-1]

    Polymorphism databases

    DMDMi143811381.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS32291.1. [P05108-1 ]
    CCDS45303.1. [P05108-2 ]
    PIRi A25922.
    RefSeqi NP_000772.2. NM_000781.2. [P05108-1 ]
    NP_001093243.1. NM_001099773.1. [P05108-2 ]
    UniGenei Hs.303980.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P05108.
    SMRi P05108. Positions 44-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107955. 4 interactions.
    IntActi P05108. 4 interactions.
    MINTi MINT-1200919.
    STRINGi 9606.ENSP00000268053.

    Chemistry

    ChEMBLi CHEMBL2033.
    DrugBanki DB00357. Aminoglutethimide.
    DB00169. Cholecalciferol.
    DB00501. Cimetidine.
    DB00257. Clotrimazole.
    DB01396. Digitoxin.
    DB00390. Digoxin.
    DB00603. Medroxyprogesterone.
    DB01092. Ouabain.
    DB00396. Progesterone.
    DB00624. Testosterone.
    DB01108. Trilostane.
    GuidetoPHARMACOLOGYi 1358.

    PTM databases

    PhosphoSitei P05108.

    Polymorphism databases

    DMDMi 143811381.

    Proteomic databases

    PaxDbi P05108.
    PRIDEi P05108.

    Protocols and materials databases

    DNASUi 1583.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268053 ; ENSP00000268053 ; ENSG00000140459 . [P05108-1 ]
    ENST00000358632 ; ENSP00000351455 ; ENSG00000140459 . [P05108-2 ]
    GeneIDi 1583.
    KEGGi hsa:1583.
    UCSCi uc002axs.2. human. [P05108-1 ]

    Organism-specific databases

    CTDi 1583.
    GeneCardsi GC15M074630.
    HGNCi HGNC:2590. CYP11A1.
    HPAi HPA016436.
    MIMi 118485. gene.
    613743. phenotype.
    neXtProti NX_P05108.
    Orphaneti 168558. 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
    289548. Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
    PharmGKBi PA27089.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000013161.
    HOVERGENi HBG051098.
    InParanoidi P05108.
    KOi K00498.
    OMAi YQRPIGV.
    OrthoDBi EOG7MKW5S.
    PhylomeDBi P05108.
    TreeFami TF105094.

    Enzyme and pathway databases

    UniPathwayi UPA00229 .
    BioCyci MetaCyc:HS06719-MONOMER.
    Reactomei REACT_11038. Pregnenolone biosynthesis.
    REACT_13812. Endogenous sterols.
    SABIO-RK P05108.

    Miscellaneous databases

    ChiTaRSi CYP11A1. human.
    EvolutionaryTracei P05108.
    GeneWikii Cholesterol_side-chain_cleavage_enzyme.
    GenomeRNAii 1583.
    NextBioi 35469259.
    PROi P05108.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05108.
    Bgeei P05108.
    CleanExi HS_CYP11A1.
    Genevestigatori P05108.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 166 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