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Database: UniProt
Entry: A0A1S3F0P8_DIPOR
LinkDB: A0A1S3F0P8_DIPOR
Original site: A0A1S3F0P8_DIPOR 
ID   A0A1S3F0P8_DIPOR        Unreviewed;      2449 AA.
AC   A0A1S3F0P8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 9.
DE   SubName: Full=acetyl-CoA carboxylase 2 {ECO:0000313|RefSeq:XP_012869770.1};
GN   Name=Acacb {ECO:0000313|RefSeq:XP_012869770.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha;
OC   Heteromyidae; Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012869770.1};
RN   [1] {ECO:0000313|RefSeq:XP_012869770.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012869770.1};
RG   RefSeq;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
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DR   RefSeq; XP_012869770.1; XM_013014316.1.
DR   GeneID; 105984210; -.
DR   CTD; 32; -.
DR   OrthoDB; 156081at2759; -.
DR   Proteomes; UP000081671; Genome assembly.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|SAAS:SAAS00296904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000081671};
KW   Ligase {ECO:0000256|SAAS:SAAS00232059};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17   2449       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010363290.
FT   DOMAIN      250    752       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      405    600       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      879    953       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN     1686   2016       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   DOMAIN     2020   2336       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
FT   REGION       47    147       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3F0P8}.
FT   REGION      159    187       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3F0P8}.
FT   COMPBIAS     47    133       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1S3F0P8}.
SQ   SEQUENCE   2449 AA;  275328 MW;  095CDD904BB8BE7D CRC64;
     MVLLLFLSCL IFSCLTFSWL KIWRKMTDSS PVTNSKLEAS LILNQEPIPA SDNSEEQLQT
     NDSDSSQPKT PKQAKPASHK SPSDACQQED SQTPHSSHDT WPTPELQVNG TGTQGPEPPD
     TYGLSSPAKP QGQRARSPTK EDKKQAHIKR QLMTNFILGS FDDNSSDEDS GAGILRESSR
     KGSRASLGTL SPEAAMIASE ADTLLPAMRP SMSGLHLVRR GREHKKLDLH RDFTVASPAE
     FVTRFGGDRV IEKVLIANNG IAAVKCMRSI RRWAYEMFRN ERAIRFVVMV TPEDLKANAE
     YIKMADQYVP VPGGPNNNNY ANVELIVDIA KRIPVQAVWA GWGHASENPK LPELLCKHGI
     AFLGPPSEAM WALGDKIAST IVAQTLQIPT LPWSGSGLTV EWAEENLQQG TPIHVPEDVY
     SLGCVKDVDE GLEAAEKIGF PLMIKASEGG GGKGIRKAES AEDFPMLFRQ VQSEIPGSPI
     FLMKLAQHAR HLEVQVLADQ YGNAVSLFGR DCSIQRRHQK IIEEAPATIA TAAVFEFMEQ
     CAVLLAKTVG YVSAGTVEYL YSQDGSFHFL ELNPRLQVEH PCTEMIADVN LPAAQLQVAM
     GVPLYRLKDI RLLYGESPWG VTPISFETPT NPPIARGHVI AARITSENPD EGFKPSSGTV
     QELNFRSSKN VWGYFSVAAA GGLHEFADSQ FGHCFSWGEN REEAISNMVV ALKELSIRGD
     FRTTVEYLIN LLETESFQNN DIDTGWLDHL IAEKVQAEKP DIMLGVVCGA LNVADAKFRD
     CMTDFLHSLE RGQVLPADSL LNIVDVELIY GGVKYILKVA RQSLTTFVLI MNGCHIEIDA
     HRLNDGGLLL SYNGNSYTTY LKEEVDSYRI TIGNKTCVFE KENDPTILRS PSAGKLTQYT
     VEDGGHVEAG SSYAEMEVMK MIMTLNVQES GHVKYIKRPG AVLEAGCVVG RLELDDPSKV
     HPAEPFTGEL PTQQTLPILG EKLHQVSHNV LENLSNIMSG YCLPEPIFSV KLKEWVQKLM
     MTLRHPSLPL LELQEIMTSV AGRIPTPVEK AVRRVMAQYA SNITSVLCQF PSQQIATILD
     CHAATLQRKA DREAFFMNTQ SIVQLVQRYR SGTRGYMKTV VLDLLRRYLN VEHYFQQAHY
     DKCVISLREQ FKPDMTQVLN CIFSHAQVAK KNQLVIMLID ELCGPDPTLS DELTSILNEL
     TQLSKSEHCK VALRARQVLI ASHLPSYELR HNQVESIFLS AIDMYGHQFC PENLKKLILS
     ETTIFDVLPT FFYHTNKVVC MASLEVYVRR GYIAYELNSL QHRELPDGTC VVEFQFMLPS
     SHPNRMVMPI SVTNPDLLRH STELFMDSGF SPLSQRMGAM VAFKRFEDFI RNFDEVISCF
     ANLPADMPLF SKARTSLYSE EDSKNLREEP IHILNVAIQC ADHLEDEALV PIFRTFVQSK
     KHILVDYGLR RITFLIAQEK EFPKFFTFRA RDEFAEDRIY RHLEPALAFQ LELSRMRNFD
     LTAVPCANHK MHLYLGAAKV KEGTEVTDHR FFVRAIVRHS DLITKEASFE YLQNEGERLL
     LEAMDELEVA FNNTSVRTDC NHIFLNFVPT VIMDPFKIEE SVRSMVMRYG SRLWKLRVLQ
     AEVKINIHQT AAGSAVPVRL FITNESGYYL DISLYKEVTD PRSGSIMFHS FGNKQGSQHG
     MLINTPYVTK DLLQAKRFQA QSLGTTYIYD FPEMFRQALF KLWSSPDKYP KDILTYTELV
     LGPQGQLVEM NRLPGGNEVG MVAFKMRMKT PEYPEGRDVV VIGNDITFRI GSFGTGEDLL
     YLRASELARA EGIPKIYLAA NSGARIGLAE EIKHMFQVAW VDPEDPHKGF KYLYLTPQDY
     TRTSSLNTVH CRHVEEGGES RYVVTDIIGK DDGLGVENLR GSGMIAGESS LAYDEIVTIS
     MVTCRALGIG AYLVRLGQRV IQVDNSHIIL TGASALNKVL GREVYTSNNQ LGGVQIMYHN
     GISHITVPDD FEGVYTILEW LSYMPKDNRS PVPIITPTDP IDRDVEFVPS RAPYDPRWML
     AGRPHPTLSG AWQSGFFDQG SFREIMAAWA QTVVTGRARL GGIPVGVIAV ETRTVEVAVP
     ADPANLDSEA KIIQQAGQVW FPDSAYKTAQ AIKDFNREKL PLLIFANWRG FSGGMKDMYD
     QVVKFGAYIV DGLRQYTQPI LIYVPPYAEL RGGSWVVLDS TINPLCIEMY ADRESRAGVL
     EPEGTVEIKF RRKDLVKTMR RIDPTYKKLV EQLGMSQLSD EDRKDLEARL KAREELLLPI
     YHQVAVQFAD LHDTPGRMLE KGVISDVLEW KTSRAFLYWR LRRRLLEDQV KREVLQASSE
     LSHDHVQSML RRWFVETEGA VKAYLWDNNQ VVVQWLEQHW LEGEGLRSTI RENIKYLKRD
     SVLKTIQGLV QKTPEVAADC TIHLSQQLSP AERAQVVKLL TSAERPAST
//
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