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B2ZZ90

- B2ZZ90_HUMAN

UniProt

B2ZZ90 - B2ZZ90_HUMAN

Protein
Submitted name:

Acetyl-Coenzyme A carboxylase alpha

Gene

ACACA

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Cofactori

    Biotin.SAAS annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: InterPro
    4. metal ion binding Source: InterPro

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: Ensembl
    2. fatty acid biosynthetic process Source: Ensembl
    3. lipid homeostasis Source: Ensembl
    4. multicellular organismal protein metabolic process Source: Ensembl
    5. protein homotetramerization Source: Ensembl
    6. tissue homeostasis Source: Ensembl

    Keywords - Molecular functioni

    LigaseSAAS annotation

    Keywords - Ligandi

    ATP-bindingSAAS annotation, BiotinUniRule annotationSAAS annotation, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Acetyl-Coenzyme A carboxylase alphaImported
    Submitted name:
    HCG30204, isoform CRA_bImported
    Gene namesi
    Name:ACACAImported
    ORF Names:hCG_30204Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24421.

    Structurei

    3D structure databases

    SMRiB2ZZ90. Positions 102-817, 1581-2338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains ATP-grasp domain.SAAS annotation
    Contains biotin carboxylation domain.SAAS annotation
    Contains biotinyl-binding domain.SAAS annotation

    Phylogenomic databases

    HOVERGENiHBG005371.
    KOiK11262.
    PhylomeDBiB2ZZ90.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B2ZZ90-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS     50
    PASVGSDTLS DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF 100
    TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA 150
    IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI 200
    PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA 250
    QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 300
    AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR 350
    LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV 400
    FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE 450
    MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC 500
    PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH 550
    EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 600
    ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN 650
    FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS 700
    CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND 750
    PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH 800
    YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH 850
    RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 900
    DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA 950
    TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ 1000
    FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG 1050
    RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV 1100
    ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL 1150
    EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 1200
    SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD 1250
    EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE 1300
    DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR 1350
    EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK 1400
    MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL 1450
    LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 1500
    SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD 1550
    SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD 1600
    IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR 1650
    LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL 1700
    RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY 1750
    LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 1800
    GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG 1850
    AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS 1900
    YMPKSVHSSV PLLNSKDPID RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW 1950
    LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD 2000
    PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS 2050
    GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 2100
    NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER 2150
    LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG 2200
    VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR 2250
    WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV 2300
    LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST 2346
    Length:2,346
    Mass (Da):265,554
    Last modified:July 22, 2008 - v1
    Checksum:iF1F0A518F8824FFC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB371587 mRNA. Translation: BAG48316.1.
    CH471199 Genomic DNA. Translation: EAW57577.1.
    CH471199 Genomic DNA. Translation: EAW57578.1.
    CH471199 Genomic DNA. Translation: EAW57581.1.
    CH471199 Genomic DNA. Translation: EAW57582.1.
    RefSeqiNP_942131.1. NM_198834.2.
    NP_942133.1. NM_198836.2.
    NP_942136.1. NM_198839.2.
    UniGeneiHs.160556.

    Genome annotation databases

    GeneIDi31.
    KEGGihsa:31.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB371587 mRNA. Translation: BAG48316.1 .
    CH471199 Genomic DNA. Translation: EAW57577.1 .
    CH471199 Genomic DNA. Translation: EAW57578.1 .
    CH471199 Genomic DNA. Translation: EAW57581.1 .
    CH471199 Genomic DNA. Translation: EAW57582.1 .
    RefSeqi NP_942131.1. NM_198834.2.
    NP_942133.1. NM_198836.2.
    NP_942136.1. NM_198839.2.
    UniGenei Hs.160556.

    3D structure databases

    SMRi B2ZZ90. Positions 102-817, 1581-2338.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 31.
    KEGGi hsa:31.

    Organism-specific databases

    CTDi 31.
    PharmGKBi PA24421.

    Phylogenomic databases

    HOVERGENi HBG005371.
    KOi K11262.
    PhylomeDBi B2ZZ90.

    Miscellaneous databases

    ChiTaRSi ACACA. human.
    GenomeRNAii 31.
    NextBioi 111.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of the human genome."
      Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
      , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
      Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE.
    3. "Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method."
      Oshikawa M., Sugai Y., Usami R., Ohtoko K., Toyama S., Kato S.
      DNA Res. 15:123-136(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.

    Entry informationi

    Entry nameiB2ZZ90_HUMAN
    AccessioniPrimary (citable) accession number: B2ZZ90
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 22, 2008
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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.