AKR1_SCHPO
ID AKR1_SCHPO Reviewed; 642 AA.
AC Q09701;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Palmitoyltransferase akr1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein akr1;
GN Name=akr1; ORFNames=SPAC2F7.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAA90497.1; -; Genomic_DNA.
DR PIR; S58154; S58154.
DR RefSeq; NP_592981.1; NM_001018381.2.
DR AlphaFoldDB; Q09701; -.
DR SMR; Q09701; -.
DR BioGRID; 278251; 27.
DR STRING; 4896.SPAC2F7.10.1; -.
DR MaxQB; Q09701; -.
DR PaxDb; Q09701; -.
DR PRIDE; Q09701; -.
DR EnsemblFungi; SPAC2F7.10.1; SPAC2F7.10.1:pep; SPAC2F7.10.
DR GeneID; 2541757; -.
DR KEGG; spo:SPAC2F7.10; -.
DR PomBase; SPAC2F7.10; akr1.
DR VEuPathDB; FungiDB:SPAC2F7.10; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_0_1; -.
DR InParanoid; Q09701; -.
DR OMA; DVPDCNG; -.
DR PhylomeDB; Q09701; -.
DR PRO; PR:Q09701; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IC:PomBase.
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; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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..642
FT /note="Palmitoyltransferase akr1"
FT /id="PRO_0000212931"
FT TOPO_DOM 1..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..496
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 1..29
FT /note="ANK 1"
FT REPEAT 33..62
FT /note="ANK 2"
FT REPEAT 67..96
FT /note="ANK 3"
FT REPEAT 100..129
FT /note="ANK 4"
FT REPEAT 133..162
FT /note="ANK 5"
FT REPEAT 166..196
FT /note="ANK 6"
FT DOMAIN 400..450
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 430
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 642 AA; 72522 MW; C83584A3300BDDA0 CRC64;
MGSLFLAASQ GELDTVKNLI SSEKIDVNAT DEGGATALHW AALNQQIPIC KFLLEHGADV
NAIGGDLQAA PIHWAAKRGS VKTVHYLVQH GADPLLKDKQ GFNCLHLAVH AASPLLVVYL
LHLDISVDLR DDQQHTPLMW ASYHGNEPIT NCLLRWGADV LATDEDKMTP LHWSIVGGNL
KCMKLILKEG GIPCTAVTAN LSGQLKTPWA LASELRVSHL FKQALISNGL KVKETSEEPE
KWVVVPSKFQ FSQKTFIIFC FLSSFIITGV FFFIMSICPM VISLIIAPLW IYFTFKYITT
CIHANIDIVH FYLETPFLAG IFSSIFFWVW CHSLLYIVPK TLPIKPLSSL LFVLISFTCI
GLYVRTAFQN PGYVDKIGAV VQRREEISKL LDKDLFNQSH YCLKCFQVKP PRSYHCGACK
RCINRYDHHC PWTGNCVGAR NHRTFLLFVF TLSTLIPIYF YVAFYYLQNI PIQKKYESYR
CLFISGTICQ WSLKDMFVLV ASLTLFVNWC WVVVLAFTQI CQVAHNVTTA EFRLFKRYGT
LVPPTKQNSS PKNGHGIHGS FLRTVCGILG LDQCILLIRE SNCFVRCFPS RAELGSQNST
SLSRNLSTVN PYDEGSIIKN CKTFWKQNFL NDGRQDEATR HV
