AKR1_SACU7
ID AKR1_SACU7 Reviewed; 763 AA.
AC Q876L5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1;
OS Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS uvarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=659244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669
RC / NRRL Y-11845;
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-759.
RC STRAIN=623-6C / CBS 9787 / CLIB 533;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(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; AACA01000384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY144796; AAO32360.1; -; Genomic_DNA.
DR AlphaFoldDB; Q876L5; -.
DR SMR; Q876L5; -.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
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; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..763
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212928"
FT TOPO_DOM 1..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..345
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..415
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..569
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 71..101
FT /note="ANK 1"
FT REPEAT 107..136
FT /note="ANK 2"
FT REPEAT 141..170
FT /note="ANK 3"
FT REPEAT 174..203
FT /note="ANK 4"
FT REPEAT 212..241
FT /note="ANK 5"
FT REPEAT 245..274
FT /note="ANK 6"
FT DOMAIN 469..519
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 499
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 763 AA; 85659 MW; 01F37BE6AD378BDB CRC64;
MTSESVTTPL ASTLVDKEQA ADHNDDSQED ISLGGSNDAT SLSSLKAIRS ENEDANETGQ
ADRNDDVEED PLLTRYHTAC QKGDLATVKE MIHGKLLEVN KDGDSVEHIT GLHWASINNR
LSVVDFLVSQ GADVNSRAGA LHATPLHWAA RYGYVYIVDF LLKHGADPTM TDDQGFNLLH
LSVNSSNIML VLYVLFSVVS KGLLDVDCQD PKGRTSLLWA AYQGDSLTVA VLLKFGANIK
IADTEGFTPL HWGTVKGQPH VLKYLIQDGA DFFQKTDAGK DCFAIAQEMN TVYSLREALI
HSGFNNDGYP IKKWFKKSQH AKLVTFLTPF VFLGLAFALF SHVNPLFAII VLFLLTLATN
KGLNKLVLPS YGRMGIHNVT LLRSPLFSGV FFGSLLWVTI VWFFKVMPWT FADEPYTNIL
LLIVLLLVFY IFGQLVTSDP GCVPEETDHE NVRQTISDLL EIGKFDTKNF CIETWARKPL
RSRFSSLNNA VVARFDHYCP WIFNDVGLKN HKGFMFFITL MECGILTFFK LCLEYFDELE
DSYEDRNQEL GKCFILGHSD LCSGLRYDRF VFLVLLWALL QSIWVASLIF VQTFQIFKGM
TNSEFNVLMK ENKANGADGV SFNENFNTTP EGFAPSIELD EDNNNTVLAP VPGSTLRKPR
TCFGVCFTVT GMDQWFAVVK ETIGIKDSSG HNIYSITSKI PTNYGWRRNV KDFWLTSDVN
APLWRRILYS PTSSKALLNG TEVDYFKLYK LPVKEAEQGS DMV
