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AB2D_ARATH
ID   AB2D_ARATH              Reviewed;         706 AA.
AC   Q6NLC1; Q9SLJ9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=ABC transporter D family member 2, chloroplastic;
DE            Short=ABC transporter ABCD.2;
DE            Short=AtABCD2;
DE            EC=7.-.-.-;
DE   Flags: Precursor;
GN   Name=ABCC2; Synonyms=PMP1; OrderedLocusNames=At1g54350; ORFNames=F20D21.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 45-57, ACETYLATION AT SER-45, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA   van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT   proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA   Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT   "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL   J. Biol. Chem. 276:30231-30244(2001).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=11855639; DOI=10.1007/s004250100661;
RA   Martinoia E., Klein M., Geisler M., Bovet L., Forestier C.,
RA   Kolukisaoglu H.U., Mueller-Roeber B., Schulz B.;
RT   "Multifunctionality of plant ABC transporters -- more than just
RT   detoxifiers.";
RL   Planta 214:345-355(2002).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA   Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA   Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA   Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT   "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL   Trends Plant Sci. 13:151-159(2008).
CC   -!- SUBUNIT: Homodimer or heterodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC       Plastid, chloroplast {ECO:0000269|PubMed:18431481}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC       Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005287; AAD25615.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33083.1; -; Genomic_DNA.
DR   EMBL; BT012226; AAS76713.1; -; mRNA.
DR   EMBL; BT012413; AAS92329.1; -; mRNA.
DR   PIR; B96585; B96585.
DR   RefSeq; NP_175837.2; NM_104313.4.
DR   AlphaFoldDB; Q6NLC1; -.
DR   SMR; Q6NLC1; -.
DR   BioGRID; 27101; 15.
DR   IntAct; Q6NLC1; 15.
DR   STRING; 3702.AT1G54350.1; -.
DR   TCDB; 3.A.1.203.8; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; Q6NLC1; -.
DR   PaxDb; Q6NLC1; -.
DR   PRIDE; Q6NLC1; -.
DR   ProteomicsDB; 245094; -.
DR   EnsemblPlants; AT1G54350.1; AT1G54350.1; AT1G54350.
DR   GeneID; 841876; -.
DR   Gramene; AT1G54350.1; AT1G54350.1; AT1G54350.
DR   KEGG; ath:AT1G54350; -.
DR   Araport; AT1G54350; -.
DR   TAIR; locus:2020138; AT1G54350.
DR   eggNOG; KOG0060; Eukaryota.
DR   HOGENOM; CLU_007587_6_0_1; -.
DR   OMA; FRYGLVH; -.
DR   OrthoDB; 309052at2759; -.
DR   PhylomeDB; Q6NLC1; -.
DR   BioCyc; ARA:AT1G54350-MON; -.
DR   PRO; PR:Q6NLC1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q6NLC1; baseline and differential.
DR   Genevisible; Q6NLC1; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IBA:GO_Central.
DR   GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR   GO; GO:0042760; P:very long-chain fatty acid catabolic process; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF06472; ABC_membrane_2; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chloroplast; Direct protein sequencing; Membrane;
KW   Nucleotide-binding; Plastid; Reference proteome; Transit peptide;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..44
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:18431481"
FT   CHAIN           45..706
FT                   /note="ABC transporter D family member 2, chloroplastic"
FT                   /id="PRO_0000379136"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          88..372
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          430..697
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          545..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         464..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         45
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:18431481"
SQ   SEQUENCE   706 AA;  80054 MW;  4E6422F72A26F7FC CRC64;
     MILMITAPVC PPHLLLRHSS LLRHESSIGN FHRKKNPRFR TVSCSSLLPQ PSVRPDKASE
     LKTLWKKFYK VASPYWFSED KDQARLRLAA VFALTLATTG ISVGFNFLGR DFYNSLANKD
     QEQFTKQLFY YLCAFAGGIP FFVLRDYTKE TLSLRWRSWM TKYYLQRYLK DQTFYKIQSQ
     SIIDNPDQRL VDDLSSFTGT ALSFSLTLVN ATIDLISFSN ILFTIYPPLF LVLLLYSFGG
     TAISVFLGKG LVNLNFLQEK KEADFRYSLV RVRENAESIA FYGGEQNEMQ LLLQRFRSAF
     DNLTELLIAS RNLEFFTDGY RYLIQILPVA VVAPMYFSGK IEFGVINQSV SAFNHILGDF
     SLVVYQFQAI SSFSAVIDRL GEFDDLLDNN IFRDPSDTVD EIELTYQSEM NSSLLDTNGS
     IKSQPNQKRL EIEELTLQTP TNGTTLVHNL SADVYDKDHL LIMGPSGSGK TSLLRAMAGL
     WRSGKGKITF YLDPEVDFTQ EKSDTQENSG KRGDVLFLPQ RPYMVLGSLR QQLLYPTWSA
     TVEETTPGGS NIDGSPPLLI REDGNEKPTT DDLMRTLEKV CLGHIADRFG GLDSIHEWSS
     VLSLGEQQRL AFARLLLSQP KLALLDESTS ALDEANEAFL YQQIQSAGIT YISIGHRRTL
     TKFHNKILQI STADPKSNER NWRIEDVDAQ DSLYGRLNQK EVPSES
 
 
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