PFA4_CRYNB
ID PFA4_CRYNB Reviewed; 459 AA.
AC P0CS69; Q55YA8; Q55YA9; Q5KLN0; Q5KLN1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
DE Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000255|HAMAP-Rule:MF_03199}; OrderedLocusNames=CNBB1070;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000255|HAMAP-Rule:MF_03199}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_03199};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0CS69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0CS69-2; Sequence=VSP_041435, VSP_041436;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
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DR EMBL; AAEY01000007; EAL22658.1; -; Genomic_DNA.
DR EMBL; AAEY01000007; EAL22657.1; -; Genomic_DNA.
DR RefSeq; XP_777304.1; XM_772211.1. [P0CS69-2]
DR RefSeq; XP_777305.1; XM_772212.1. [P0CS69-1]
DR AlphaFoldDB; P0CS69; -.
DR SMR; P0CS69; -.
DR EnsemblFungi; AAW41652; AAW41652; CNB04690.
DR EnsemblFungi; EAL22657; EAL22657; CNBB1070. [P0CS69-2]
DR EnsemblFungi; EAL22658; EAL22658; CNBB1070. [P0CS69-1]
DR GeneID; 4934197; -.
DR KEGG; cnb:CNBB1070; -.
DR VEuPathDB; FungiDB:CNBB1070; -.
DR HOGENOM; CLU_027721_7_1_1; -.
DR Proteomes; UP000001435; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum 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-UniRule.
DR GO; GO:0018345; P:protein palmitoylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Palmitate; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..459
FT /note="Palmitoyltransferase PFA4"
FT /id="PRO_0000410347"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 31..37
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 59..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 160..177
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 199..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT DOMAIN 95..145
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 278..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT VAR_SEQ 277..340
FT /note="DHTTQYFWPPQDPSRLPNPPPIPAHASPFVYGNNGFNPNLQPTNSLRARRSS
FT TPHIDEDEHSHE -> GESATVEWAGIVAPREGSSAPGEYGAADQCESAGSGSGTNGRP
FT GMGHGEERVRHGRARVEHSMV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041435"
FT VAR_SEQ 341..459
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041436"
SQ SEQUENCE 459 AA; 52818 MW; 02B30A4824C3E7E4 CRC64;
MAARNWSRVW VGGTVILISF IAFSSQIFVI WPWYGREISL DLLKLLVPLN LAAFMIFWNY
RLCVITSPGS VPEGWRPNIG AMDGMEVKKG THTPRYCKNC EHYKPPRAHH CRQCKTCWLK
LDHHCPWIGN CVGFYNQGHF IRFLLWVDIG TTFHLIIMVR RVLYIAEYYH QEPTLADVLF
LVFNFATCVP VWLCVGMFSI YHVYLACGNS TTIEGWEKDK VATLIRRGKI KEVKYPYNIG
IYKNIKSVLG PNPFLWLWPQ KMQGDGLSFP VNPSAGDHTT QYFWPPQDPS RLPNPPPIPA
HASPFVYGNN GFNPNLQPTN SLRARRSSTP HIDEDEHSHE RDQYRHYSSG EERDNDSIST
SSSPKPYLSD YDHYDEGPMY PGERMTALIP RVRRGSEGWE VAPGGGWNAY SGMMDEEVGW
DDEVGYDEAP GEGPYVERPW EMRGRYNVYD TEEESGYAH
