ZDH14_HUMAN
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 03-AUG-2022, entry version 150.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; Q8IZN3; -.
DR PeptideAtlas; Q8IZN3; -.
DR PRIDE; Q8IZN3; -.
DR ProteomicsDB; 71377; -. [Q8IZN3-1]
DR ProteomicsDB; 71378; -. [Q8IZN3-2]
DR Antibodypedia; 33428; 61 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 CTD; 79683; -.
DR DisGeNET; 79683; -.
DR GeneCards; ZDHHC14; -.
DR HGNC; HGNC:20341; ZDHHC14.
DR HPA; ENSG00000175048; Tissue enhanced (brain).
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; SVPKRKW; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q8IZN3; -.
DR TreeFam; TF312923; -.
DR PathwayCommons; Q8IZN3; -.
DR BioGRID-ORCS; 79683; 8 hits in 1079 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 165 other tissues.
DR ExpressionAtlas; Q8IZN3; baseline and differential.
DR Genevisible; Q8IZN3; 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:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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: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 Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
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
