ID   ZDH14_HUMAN             Reviewed;         488 AA.
AC   Q8IZN3; A6NDB7; Q5JS07; Q5JS08; Q6PHS4; Q8IZN2; Q9H7F1;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Palmitoyltransferase ZDHHC14 {ECO:0000305|PubMed:27481942};
DE            EC=2.3.1.225 {ECO:0000305|PubMed:27481942};
DE   AltName: Full=DHHC domain-containing cysteine-rich protein 14 {ECO:0000303|PubMed:16647879};
DE            Short=DHHC-14 {ECO:0000303|PubMed:16647879};
DE   AltName: Full=NEW1 domain-containing protein {ECO:0000303|Ref.1};
DE            Short=NEW1CP {ECO:0000303|Ref.1};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 14 {ECO:0000312|HGNC:HGNC:20341};
GN   Name=ZDHHC14 {ECO:0000312|HGNC:HGNC:20341};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Stomach;
RA   Guo J.H., Chen L., Yu L.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-488 (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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-488 (ISOFORM 1).
RC   TISSUE=Brain;
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, AND TISSUE SPECIFICITY.
RX   PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA   Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT   "Intracellular localization and tissue-specific distribution of human and
RT   yeast DHHC cysteine-rich domain-containing proteins.";
RL   Biochim. Biophys. Acta 1761:474-483(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   FUNCTION.
RX   PubMed=21151021; DOI=10.1038/leu.2010.271;
RA   Yu L., Reader J.C., Chen C., Zhao X.F., Ha J.S., Lee C., York T., Gojo I.,
RA   Baer M.R., Ning Y.;
RT   "Activation of a novel palmitoyltransferase ZDHHC14 in acute biphenotypic
RT   leukemia and subsets of acute myeloid leukemia.";
RL   Leukemia 25:367-371(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   FUNCTION.
RX   PubMed=24407904; DOI=10.1002/path.4327;
RA   Yeste-Velasco M., Mao X., Grose R., Kudahetti S.C., Lin D., Marzec J.,
RA   Vasiljevic N., Chaplin T., Xue L., Xu M., Foster J.M., Karnam S.S.,
RA   James S.Y., Chioni A.M., Gould D., Lorincz A.T., Oliver R.T., Chelala C.,
RA   Thomas G.M., Shipley J.M., Mather S.J., Berney D.M., Young B.D., Lu Y.J.;
RT   "Identification of ZDHHC14 as a novel human tumour suppressor gene.";
RL   J. Pathol. 232:566-577(2014).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=27481942; DOI=10.1074/jbc.m116.725762;
RA   Adachi N., Hess D.T., McLaughlin P., Stamler J.S.;
RT   "S-Palmitoylation of a Novel Site in the beta2-Adrenergic Receptor
RT   Associated with a Novel Intracellular Itinerary.";
RL   J. Biol. Chem. 291:20232-20246(2016).
CC   -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC       palmitate onto various protein substrates. May have a
CC       palmitoyltransferase activity toward the beta-2 adrenergic
CC       receptor/ADRB2 and thereby regulate G protein-coupled receptor
CC       signaling (PubMed:27481942). May play a role in cell differentiation
CC       and apoptosis (PubMed:21151021, PubMed:24407904).
CC       {ECO:0000269|PubMed:21151021, ECO:0000269|PubMed:24407904,
CC       ECO:0000269|PubMed:27481942}.
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:27481942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000305|PubMed:27481942};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000305|PubMed:27481942}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IZN3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IZN3-2; Sequence=VSP_008651;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16647879}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q8IUH5}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF542388; AAN47142.1; -; mRNA.
DR   EMBL; AF542389; AAN47143.1; -; mRNA.
DR   EMBL; AL450328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL117344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47671.1; -; Genomic_DNA.
DR   EMBL; AK024637; BAB14941.1; ALT_INIT; mRNA.
DR   EMBL; BC056399; AAH56399.1; -; mRNA.
DR   CCDS; CCDS47510.1; -. [Q8IZN3-2]
DR   CCDS; CCDS5252.1; -. [Q8IZN3-1]
DR   RefSeq; NP_078906.2; NM_024630.2. [Q8IZN3-1]
DR   RefSeq; NP_714968.1; NM_153746.1. [Q8IZN3-2]
DR   AlphaFoldDB; Q8IZN3; -.
DR   BioGRID; 122806; 5.
DR   STRING; 9606.ENSP00000352821; -.
DR   iPTMnet; Q8IZN3; -.
DR   PhosphoSitePlus; Q8IZN3; -.
DR   SwissPalm; Q8IZN3; -.
DR   BioMuta; ZDHHC14; -.
DR   DMDM; 37999849; -.
DR   EPD; Q8IZN3; -.
DR   jPOST; Q8IZN3; -.
DR   MassIVE; Q8IZN3; -.
DR   MaxQB; Q8IZN3; -.
DR   PaxDb; 9606-ENSP00000352821; -.
DR   PeptideAtlas; Q8IZN3; -.
DR   ProteomicsDB; 71377; -. [Q8IZN3-1]
DR   ProteomicsDB; 71378; -. [Q8IZN3-2]
DR   Pumba; Q8IZN3; -.
DR   Antibodypedia; 33428; 78 antibodies from 19 providers.
DR   DNASU; 79683; -.
DR   Ensembl; ENST00000359775.10; ENSP00000352821.5; ENSG00000175048.17. [Q8IZN3-1]
DR   Ensembl; ENST00000414563.6; ENSP00000410713.2; ENSG00000175048.17. [Q8IZN3-2]
DR   GeneID; 79683; -.
DR   KEGG; hsa:79683; -.
DR   MANE-Select; ENST00000359775.10; ENSP00000352821.5; NM_024630.3; NP_078906.2.
DR   UCSC; uc003qqs.4; human. [Q8IZN3-1]
DR   AGR; HGNC:20341; -.
DR   CTD; 79683; -.
DR   DisGeNET; 79683; -.
DR   GeneCards; ZDHHC14; -.
DR   HGNC; HGNC:20341; ZDHHC14.
DR   HPA; ENSG00000175048; Low tissue specificity.
DR   MIM; 619295; gene.
DR   neXtProt; NX_Q8IZN3; -.
DR   OpenTargets; ENSG00000175048; -.
DR   PharmGKB; PA134935513; -.
DR   VEuPathDB; HostDB:ENSG00000175048; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   GeneTree; ENSGT00940000156483; -.
DR   HOGENOM; CLU_018741_0_0_1; -.
DR   InParanoid; Q8IZN3; -.
DR   OMA; HSRTMHI; -.
DR   OrthoDB; 5480099at2759; -.
DR   PhylomeDB; Q8IZN3; -.
DR   TreeFam; TF312923; -.
DR   PathwayCommons; Q8IZN3; -.
DR   BioGRID-ORCS; 79683; 8 hits in 1157 CRISPR screens.
DR   ChiTaRS; ZDHHC14; human.
DR   GenomeRNAi; 79683; -.
DR   Pharos; Q8IZN3; Tbio.
DR   PRO; PR:Q8IZN3; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8IZN3; Protein.
DR   Bgee; ENSG00000175048; Expressed in C1 segment of cervical spinal cord and 167 other cell types or tissues.
DR   ExpressionAtlas; Q8IZN3; baseline and differential.
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:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF28; PALMITOYLTRANSFERASE ZDHHC14; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
DR   Genevisible; Q8IZN3; HS.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW   Golgi apparatus; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Palmitoyltransferase ZDHHC14"
FT                   /id="PRO_0000212891"
FT   TOPO_DOM        1..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..255
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..488
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          165..215
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        195
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         357..371
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_008651"
FT   VARIANT         334
FT                   /note="T -> M (in dbSNP:rs8180688)"
FT                   /id="VAR_034586"
SQ   SEQUENCE   488 AA;  53388 MW;  B50CCDE1B738C135 CRC64;
     MPPGGGGPMK DCEYSQISTH SSSPMESPHK KKKIAARRKW EVFPGRNKFF CNGRIMMARQ
     TGVFYLTLVL ILVTSGLFFA FDCPYLAVKI TPAIPAVAGI LFFFVMGTLL RTSFSDPGVL
     PRATPDEAAD LERQIDIANG TSSGGYRPPP RTKEVIINGQ TVKLKYCFTC KIFRPPRASH
     CSLCDNCVER FDHHCPWVGN CVGKRNYRFF YMFILSLSFL TVFIFAFVIT HVILRSQQTG
     FLNALKDSPA SVLEAVVCFF SVWSIVGLSG FHTYLISSNQ TTNEDIKGSW SNKRGKENYN
     PYSYGNIFTN CCVALCGPIS PSLIDRRGYI QPDTPQPAAP SNGITMYGAT QSQSDMCDQD
     QCIQSTKFVL QAAATPLLQS EPSLTSDELH LPGKPGLGTP CASLTLGPPT PPASMPNLAE
     ATLADVMPRK DEHMGHQFLT PDEAPSPPRL LAAGSPLAHS RTMHVLGLAS QDSLHEDSVR
     GLVKLSSV
//