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AKR1_NEUCR
ID   AKR1_NEUCR              Reviewed;         729 AA.
AC   Q7S3M5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Palmitoyltransferase akr1;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein akr1;
DE   AltName: Full=Palmitoyltransferase 1;
GN   Name=ptr-1; Synonyms=akr1; ORFNames=NCU08218;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane
CC       protein. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR   EMBL; CM002238; EAA30072.3; -; Genomic_DNA.
DR   RefSeq; XP_959308.3; XM_954215.3.
DR   AlphaFoldDB; Q7S3M5; -.
DR   SMR; Q7S3M5; -.
DR   STRING; 5141.EFNCRP00000004752; -.
DR   EnsemblFungi; EAA30072; EAA30072; NCU08218.
DR   GeneID; 3875430; -.
DR   KEGG; ncr:NCU08218; -.
DR   VEuPathDB; FungiDB:NCU08218; -.
DR   HOGENOM; CLU_012510_1_0_1; -.
DR   InParanoid; Q7S3M5; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..729
FT                   /note="Palmitoyltransferase akr1"
FT                   /id="PRO_0000212927"
FT   TOPO_DOM        1..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..354
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..383
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..483
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..534
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        556..729
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          76..105
FT                   /note="ANK 1"
FT   REPEAT          110..139
FT                   /note="ANK 2"
FT   REPEAT          143..172
FT                   /note="ANK 3"
FT   REPEAT          176..205
FT                   /note="ANK 4"
FT   REPEAT          209..238
FT                   /note="ANK 5"
FT   DOMAIN          440..490
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        470
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   729 AA;  80085 MW;  0F11B0993956E381 CRC64;
     MVHHDGADAH AGHAAPAQPP MKSDTATPKL NSEVELGSLP SEAHNDIMQM ARVGDITGME
     KLFAAGEYDA TYSDDEGITP LHWAAINNQY AMCKFLIDKG AEINKKGGES VATPLQWAAQ
     RCHYYTVHLL LQHGADPLIT DSQGYNTLHI STFNGNVLLI VLLLHQGIPV DVEDAYGHTA
     LMWSAYKGFP ACVDVFLRWG ASVHAKDEQG FTALHWALVK GSPGCIQKLI EYGADRFAKT
     ANGKTPAITA QELNTVAAWQ KALDECGYDE HGNAIVPSWP GASYLLQDRR SFMTKFTFLW
     PFVMVWATMV VMAGMPVFVG IPLGVLAGYA VQWVAQQVIA YAPPDMRQLQ KTPWMAGIFA
     GSLFLCIMNW LLHIFGSTMF GQDSAVIPNL LFAFFISMTI WFYIRCMVDD PGFVPKMGGV
     AEQKAVIDEL ISLWKFDESN FCVTCMIRTP LRSKHCRRCQ RCVAKHDHHC PWVYNCIGVN
     NHRHFFFYLI NLTLSVVTYD WLTYRYLSTL SETASDECNI LAPSLCRIVN ADTYSLLTAI
     WASLQLTWVS MLLFVQFVQV SSAMTTYENM HGIDNYSATS LNSSFTSTGA PLNPPSLPAP
     GPSPAAGGAR HGGRHAHGHN HKQGFIKQWS RLLGVDAFIE TAAGRGATTG KGSKRNKRGN
     PYSRGCVTNC KDFWCDPSPM FGKHENGAAV LGGVPVNYTD MYESPGVMTS GGGGRRRGGG
     YESVAGEEV
 
 
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