ID GALT5_HUMAN Reviewed; 940 AA.
AC Q7Z7M9; A5PKZ1; Q9UGK7; Q9UHL6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 5;
DE Short=GalNAc-T5;
DE Short=pp-GaNTase 5;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
GN Name=GALNT5;
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].
RA Huang C.Q., Wu S.L., Cheng Z.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovium;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 273-940.
RA Bennett E.P.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 331-940, AND INTERACTION WITH EXT2.
RX PubMed=10545594; DOI=10.1093/hmg/8.12.2155;
RA Simmons A.D., Musy M.M., Lopes C.S., Hwang L.-Y., Yang Y.-P., Lovett M.;
RT "A direct interaction between EXT proteins and glycosyltransferases is
RT defective in hereditary multiple exostoses.";
RL Hum. Mol. Genet. 8:2155-2164(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP VARIANTS [LARGE SCALE ANALYSIS] ASP-507 AND PHE-692.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward EA2 peptide substrate, but has a weak activity toward Muc2 or
CC Muc1b substrates (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with EXT2. Does not interact with EXT1, EXTL1 or
CC EXTL3. {ECO:0000269|PubMed:10545594}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_487";
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DR EMBL; AY277591; AAP34404.1; -; mRNA.
DR EMBL; AK292154; BAF84843.1; -; mRNA.
DR EMBL; CH471058; EAX11449.1; -; Genomic_DNA.
DR EMBL; BC142676; AAI42677.1; -; mRNA.
DR EMBL; AJ245539; CAB65104.1; -; mRNA.
DR EMBL; AF154107; AAF15313.1; -; mRNA.
DR CCDS; CCDS2203.1; -.
DR RefSeq; NP_001316797.1; NM_001329868.1.
DR RefSeq; NP_055383.1; NM_014568.2.
DR AlphaFoldDB; Q7Z7M9; -.
DR SMR; Q7Z7M9; -.
DR BioGRID; 116394; 36.
DR IntAct; Q7Z7M9; 6.
DR MINT; Q7Z7M9; -.
DR STRING; 9606.ENSP00000259056; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyCosmos; Q7Z7M9; 12 sites, No reported glycans.
DR GlyGen; Q7Z7M9; 54 sites, 1 O-linked glycan (42 sites).
DR iPTMnet; Q7Z7M9; -.
DR PhosphoSitePlus; Q7Z7M9; -.
DR BioMuta; GALNT5; -.
DR DMDM; 51315940; -.
DR CPTAC; CPTAC-2216; -.
DR jPOST; Q7Z7M9; -.
DR MassIVE; Q7Z7M9; -.
DR MaxQB; Q7Z7M9; -.
DR PaxDb; 9606-ENSP00000259056; -.
DR PeptideAtlas; Q7Z7M9; -.
DR ProteomicsDB; 69571; -.
DR Pumba; Q7Z7M9; -.
DR Antibodypedia; 2453; 115 antibodies from 21 providers.
DR DNASU; 11227; -.
DR Ensembl; ENST00000259056.5; ENSP00000259056.4; ENSG00000136542.9.
DR GeneID; 11227; -.
DR KEGG; hsa:11227; -.
DR MANE-Select; ENST00000259056.5; ENSP00000259056.4; NM_014568.3; NP_055383.1.
DR UCSC; uc002tzg.4; human.
DR AGR; HGNC:4127; -.
DR CTD; 11227; -.
DR DisGeNET; 11227; -.
DR GeneCards; GALNT5; -.
DR HGNC; HGNC:4127; GALNT5.
DR HPA; ENSG00000136542; Tissue enhanced (intestine, lung, stomach).
DR MIM; 615129; gene.
DR neXtProt; NX_Q7Z7M9; -.
DR OpenTargets; ENSG00000136542; -.
DR PharmGKB; PA28540; -.
DR VEuPathDB; HostDB:ENSG00000136542; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR InParanoid; Q7Z7M9; -.
DR OMA; HGMHHVL; -.
DR OrthoDB; 202750at2759; -.
DR PhylomeDB; Q7Z7M9; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q7Z7M9; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q7Z7M9; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 11227; 13 hits in 1151 CRISPR screens.
DR ChiTaRS; GALNT5; human.
DR GenomeRNAi; 11227; -.
DR Pharos; Q7Z7M9; Tbio.
DR PRO; PR:Q7Z7M9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7Z7M9; Protein.
DR Bgee; ENSG00000136542; Expressed in nasal cavity epithelium and 117 other cell types or tissues.
DR Genevisible; Q7Z7M9; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11675:SF130; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 5; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..940
FT /note="Polypeptide N-acetylgalactosaminyltransferase 5"
FT /id="PRO_0000059110"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..940
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 804..935
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 131..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..604
FT /note="Catalytic subdomain A"
FT REGION 664..726
FT /note="Catalytic subdomain B"
FT COMPBIAS 151..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 590
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 695
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 486..718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 709..789
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 822..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 858..873
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 908..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VARIANT 77
FT /note="P -> L (in dbSNP:rs3739112)"
FT /id="VAR_019578"
FT VARIANT 489
FT /note="Q -> H (in dbSNP:rs6759356)"
FT /id="VAR_019579"
FT VARIANT 507
FT /note="E -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035991"
FT VARIANT 692
FT /note="L -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035992"
FT CONFLICT 273..275
FT /note="NTS -> AEG (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 940 AA; 106266 MW; DB2DFACDCACD0F6A CRC64;
MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV RRERIGFRVQ
PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK VEVDLDQTQR ERKMQNALGR
GKVVPLWHPA HLQTLPVTPN KQKTDGRGTK PEASSHQGTP KQTTAQGAPK TSFIAAKGTQ
VVKISVHMGR VSLKQEPRKS HSPSSDTSKL AAERDLNVTI SLSTDRPKQR SQAVANERAH
PASTAVPKSG EAMALNKTKT QSKEVNANKH KANTSLPFPK FTVNSNRLRK QSINETPLGS
LSKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV LGKSQSKHIS
RNRSEMSSSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA PSTEYNQSHI KALLPEDSGT
HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG KEKEAERRWK EGNFNVYLSD LIPVDRAIED
TRPAGCAEQL VHNNLPTTSV IMCFVDEVWS TLLRSVHSVI NRSPPHLIKE ILLVDDFSTK
DYLKDNLDKY MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP PDVIAKNRIK
ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR
VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ
RELRKKLKCK SFKWYLENVF PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE
LQQFNYTWLR LIKCGEWCIA PIPDKGAVRL HPCDNRNKGL KWLHKSTSVF HPELVNHIVF
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA
//
