ZDHC6_HUMAN
ID ZDHC6_HUMAN Reviewed; 413 AA.
AC Q9H6R6; D3DRB6; Q53G45; Q96IV7; Q9H605;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Palmitoyltransferase ZDHHC6 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000305|PubMed:22314232};
DE AltName: Full=Stearoyltransferase ZDHHC6 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:26214738};
DE AltName: Full=Transmembrane protein H4 {ECO:0000303|Ref.1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 6 {ECO:0000303|PubMed:22314232};
DE Short=DHHC-6 {ECO:0000303|PubMed:22314232};
DE AltName: Full=Zinc finger protein 376;
GN Name=ZDHHC6 {ECO:0000312|HGNC:HGNC:19160};
GN Synonyms=ZNF376 {ECO:0000312|HGNC:HGNC:19160};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yang Y.C., Chen S.Y., Chang M.S.;
RT "H4, a novel protein containing 4 transmembrane domains.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLU-409; LYS-410; LYS-411;
RP ASN-412 AND ARG-413.
RX PubMed=21926431; DOI=10.1074/jbc.m111.272369;
RA Gorleku O.A., Barns A.M., Prescott G.R., Greaves J., Chamberlain L.H.;
RT "Endoplasmic reticulum localization of DHHC palmitoyltransferases mediated
RT by lysine-based sorting signals.";
RL J. Biol. Chem. 286:39573-39584(2011).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22314232; DOI=10.1038/emboj.2012.15;
RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A.,
RA Dal Peraro M., van der Goot F.G.;
RT "Palmitoylated calnexin is a key component of the ribosome-translocon
RT complex.";
RL EMBO J. 31:1823-1835(2012).
RN [8]
RP FUNCTION.
RX PubMed=22728137; DOI=10.1016/j.febslet.2012.06.011;
RA Fairbank M., Huang K., El-Husseini A., Nabi I.R.;
RT "RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin
RT ligase.";
RL FEBS Lett. 586:2488-2493(2012).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26214738; DOI=10.1038/nature14601;
RA Senyilmaz D., Virtue S., Xu X., Tan C.Y., Griffin J.L., Miller A.K.,
RA Vidal-Puig A., Teleman A.A.;
RT "Regulation of mitochondrial morphology and function by stearoylation of
RT TFR1.";
RL Nature 525:124-128(2015).
RN [10]
RP FUNCTION, AND INTERACTION WITH SELENOK.
RX PubMed=25368151; DOI=10.1073/pnas.1417176111;
RA Fredericks G.J., Hoffmann F.W., Rose A.H., Osterheld H.J., Hess F.M.,
RA Mercier F., Hoffmann P.R.;
RT "Stable expression and function of the inositol 1,4,5-triphosphate receptor
RT requires palmitoylation by a DHHC6/selenoprotein K complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16478-16483(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, PALMITOYLATION AT CYS-328; CYS-329
RP AND CYS-343, AND MUTAGENESIS OF 328-CYS-CYS-329 AND CYS-343.
RX PubMed=28826475; DOI=10.7554/elife.27826;
RA Abrami L., Dallavilla T., Sandoz P.A., Demir M., Kunz B., Savoglidis G.,
RA Hatzimanikatis V., van der Goot F.G.;
RT "Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation
RT cascade.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Endoplasmic reticulum palmitoyl acyltransferase that mediates
CC palmitoylation of proteins such as AMFR, CALX, ITPR1 and TFRC
CC (PubMed:22314232, PubMed:22728137, PubMed:25368151, PubMed:28826475).
CC Palmitoylates calnexin (CALX), which is required for its association
CC with the ribosome-translocon complex and efficient folding of
CC glycosylated proteins (PubMed:22314232). Mediates palmitoylation of
CC AMFR, promoting AMFR distribution to the peripheral endoplasmic
CC reticulum (PubMed:22728137). Together with SELENOK, palmitoylates ITPR1
CC in immune cells, leading to regulate ITPR1 stability and function
CC (PubMed:25368151). Stearoyltransferase that mediates stearoylation of
CC TFRC to inhibit TFRC-mediated activation of the JNK pathway and
CC mitochondrial fragmentation (PubMed:26214738).
CC {ECO:0000269|PubMed:22314232, ECO:0000269|PubMed:22728137,
CC ECO:0000269|PubMed:25368151, ECO:0000269|PubMed:26214738,
CC ECO:0000269|PubMed:28826475}.
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:0000305|PubMed:22314232};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:22314232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000305|PubMed:26214738};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000305|PubMed:26214738};
CC -!- SUBUNIT: Homooligomerizes (PubMed:28826475). Interacts with SELENOK
CC (PubMed:25368151). {ECO:0000269|PubMed:25368151,
CC ECO:0000269|PubMed:28826475}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21926431, ECO:0000269|PubMed:22314232,
CC ECO:0000269|PubMed:28826475}; Multi-pass membrane protein
CC {ECO:0000255}. Note=When not palmitoylated, accumulates to dot-like
CC structures in the endoplasmic reticulum (PubMed:28826475).
CC {ECO:0000269|PubMed:28826475}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H6R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6R6-2; Sequence=VSP_006938;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum
CC localization. {ECO:0000269|PubMed:21926431}.
CC -!- PTM: Palmitoylated at 3 different sites by ZDHHC16 (PubMed:28826475).
CC The combination of the different palmitoylation events strongly affects
CC the quaternary assembly of ZDHHC6, its localization, stability and
CC function (PubMed:28826475). Palmitoylation at Cys-328 accelerates the
CC turnover of ZDHHC6 (PubMed:28826475). Depalmitoylated by LYPLA2
CC (PubMed:28826475). {ECO:0000269|PubMed:28826475}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF267740; AAL56663.1; -; mRNA.
DR EMBL; AK025605; BAB15187.1; -; mRNA.
DR EMBL; AK026369; BAB15462.1; ALT_INIT; mRNA.
DR EMBL; AK223086; BAD96806.1; -; mRNA.
DR EMBL; CH471066; EAW49526.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49528.1; -; Genomic_DNA.
DR EMBL; BC007213; AAH07213.1; -; mRNA.
DR EMBL; BC017434; AAH17434.1; -; mRNA.
DR CCDS; CCDS7574.1; -. [Q9H6R6-1]
DR CCDS; CCDS76335.1; -. [Q9H6R6-2]
DR RefSeq; NP_001290063.1; NM_001303134.1. [Q9H6R6-2]
DR RefSeq; NP_071939.1; NM_022494.2. [Q9H6R6-1]
DR RefSeq; XP_005270108.1; XM_005270051.4.
DR RefSeq; XP_006718011.1; XM_006717948.3.
DR RefSeq; XP_016872050.1; XM_017016561.1.
DR RefSeq; XP_016872051.1; XM_017016562.1. [Q9H6R6-2]
DR RefSeq; XP_016872052.1; XM_017016563.1. [Q9H6R6-2]
DR AlphaFoldDB; Q9H6R6; -.
DR BioGRID; 122177; 61.
DR CORUM; Q9H6R6; -.
DR IntAct; Q9H6R6; 18.
DR MINT; Q9H6R6; -.
DR STRING; 9606.ENSP00000358413; -.
DR iPTMnet; Q9H6R6; -.
DR PhosphoSitePlus; Q9H6R6; -.
DR SwissPalm; Q9H6R6; -.
DR BioMuta; ZDHHC6; -.
DR DMDM; 28202106; -.
DR EPD; Q9H6R6; -.
DR jPOST; Q9H6R6; -.
DR MassIVE; Q9H6R6; -.
DR MaxQB; Q9H6R6; -.
DR PaxDb; Q9H6R6; -.
DR PeptideAtlas; Q9H6R6; -.
DR PRIDE; Q9H6R6; -.
DR ProteomicsDB; 81020; -. [Q9H6R6-1]
DR ProteomicsDB; 81021; -. [Q9H6R6-2]
DR Antibodypedia; 18429; 98 antibodies from 17 providers.
DR DNASU; 64429; -.
DR Ensembl; ENST00000369404.3; ENSP00000358412.3; ENSG00000023041.12. [Q9H6R6-2]
DR Ensembl; ENST00000369405.7; ENSP00000358413.3; ENSG00000023041.12. [Q9H6R6-1]
DR Ensembl; ENST00000683895.1; ENSP00000507661.1; ENSG00000023041.12. [Q9H6R6-1]
DR Ensembl; ENST00000684507.1; ENSP00000507009.1; ENSG00000023041.12. [Q9H6R6-1]
DR GeneID; 64429; -.
DR KEGG; hsa:64429; -.
DR MANE-Select; ENST00000369405.7; ENSP00000358413.3; NM_022494.3; NP_071939.1.
DR UCSC; uc001kzv.3; human. [Q9H6R6-1]
DR CTD; 64429; -.
DR DisGeNET; 64429; -.
DR GeneCards; ZDHHC6; -.
DR HGNC; HGNC:19160; ZDHHC6.
DR HPA; ENSG00000023041; Low tissue specificity.
DR MIM; 618715; gene.
DR neXtProt; NX_Q9H6R6; -.
DR OpenTargets; ENSG00000023041; -.
DR PharmGKB; PA38803; -.
DR VEuPathDB; HostDB:ENSG00000023041; -.
DR eggNOG; KOG1314; Eukaryota.
DR GeneTree; ENSGT00940000155642; -.
DR InParanoid; Q9H6R6; -.
DR OMA; FIYPYDL; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q9H6R6; -.
DR TreeFam; TF320809; -.
DR PathwayCommons; Q9H6R6; -.
DR SignaLink; Q9H6R6; -.
DR BioGRID-ORCS; 64429; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; ZDHHC6; human.
DR GenomeRNAi; 64429; -.
DR Pharos; Q9H6R6; Tbio.
DR PRO; PR:Q9H6R6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H6R6; protein.
DR Bgee; ENSG00000023041; Expressed in renal glomerulus and 198 other tissues.
DR ExpressionAtlas; Q9H6R6; baseline and differential.
DR Genevisible; Q9H6R6; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0140438; P:protein stearoylation; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; SH3 domain; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..413
FT /note="Palmitoyltransferase ZDHHC6"
FT /id="PRO_0000212871"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..57
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..205
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 99..149
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT DOMAIN 313..398
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOTIF 410..413
FT /note="Di-lysine motif"
FT /evidence="ECO:0000269|PubMed:21926431"
FT ACT_SITE 129
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT LIPID 328
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:28826475"
FT LIPID 329
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:28826475"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:28826475"
FT VAR_SEQ 90..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006938"
FT VARIANT 41
FT /note="D -> N (in dbSNP:rs34350728)"
FT /id="VAR_052974"
FT MUTAGEN 328..329
FT /note="CC->AA: Abolishes palmitoylation, leading to
FT impaired homooligomeization and decreased catalytic
FT activity; when associated with A-343."
FT /evidence="ECO:0000269|PubMed:28826475"
FT MUTAGEN 343
FT /note="C->A: Abolishes palmitoylation, leading to impaired
FT homooligomeization and decreased catalytic activity; when
FT associated with 328-A-A-329."
FT /evidence="ECO:0000269|PubMed:28826475"
FT MUTAGEN 409
FT /note="E->A: Does not affect localization to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:21926431"
FT MUTAGEN 410
FT /note="K->A: Impaired localization to the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:21926431"
FT MUTAGEN 411
FT /note="K->A: Impaired localization to the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:21926431"
FT MUTAGEN 412
FT /note="N->A: Does not affect localization to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:21926431"
FT MUTAGEN 413
FT /note="R->A: Does not affect localization to the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:21926431"
FT CONFLICT 57
FT /note="N -> S (in Ref. 3; BAD96806)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="V -> I (in Ref. 3; BAD96806)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="V -> A (in Ref. 3; BAD96806)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="P -> L (in Ref. 2; BAB15462)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> G (in Ref. 2; BAB15462)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="S -> P (in Ref. 3; BAD96806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47663 MW; E4C6CD875FA03713 CRC64;
MGTFCSVIKF ENLQELKRLC HWGPIIALGV IAICSTMAMI DSVLWYWPLH TTGGSVNFIM
LINWTVMILY NYFNAMFVGP GFVPLGWKPE ISQDTMYLQY CKVCQAYKAP RSHHCRKCNR
CVMKMDHHCP WINNCCGYQN HASFTLFLLL APLGCIHAAF IFVMTMYTQL YHRLSFGWNT
VKIDMSAARR DPLPIVPFGL AAFATTLFAL GLALGTTIAV GMLFFIQMKI ILRNKTSIES
WIEEKAKDRI QYYQLDEVFV FPYDMGSRWR NFKQVFTWSG VPEGDGLEWP VREGCHQYSL
TIEQLKQKAD KRVRSVRYKV IEDYSGACCP LNKGIKTFFT SPCTEEPRIQ LQKGEFILAT
RGLRYWLYGD KILDDSFIEG VSRIRGWFPR KCVEKCPCDA ETDQAPEGEK KNR
