ID   GALT7_HUMAN             Reviewed;         657 AA.
AC   Q86SF2; B3KQU3; Q7Z5W7; Q9UJ28;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=N-acetylgalactosaminyltransferase 7;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
DE   AltName: Full=Polypeptide GalNAc transferase 7;
DE            Short=GalNAc-T7;
DE            Short=pp-GaNTase 7;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
GN   Name=GALNT7;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=10544240; DOI=10.1016/s0014-5793(99)01268-5;
RA   Bennett E.P., Hassan H., Hollingsworth M.A., Clausen H.;
RT   "A novel human UDP-N-acetyl-D-galactosamine;polypeptide N-
RT   acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial
RT   GalNAc-glycosylated acceptor substrates.";
RL   FEBS Lett. 460:226-230(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
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].
RC   TISSUE=Placenta, and Testis;
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   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=11925450; DOI=10.1074/jbc.m202684200;
RA   Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A.,
RA   Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R.,
RA   Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A.,
RA   Clausen H.;
RT   "Functional conservation of subfamilies of putative UDP-N-
RT   acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
RT   Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of
RT   l(2)35Aa is essential in Drosophila.";
RL   J. Biol. Chem. 277:22623-22638(2002).
RN   [6]
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).
CC   -!- FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide
CC       biosynthesis, which catalyzes the transfer of an N-acetyl-D-
CC       galactosamine residue to an already glycosylated peptide. In contrast
CC       to other proteins of the family, it does not act as a peptide
CC       transferase that transfers GalNAc onto serine or threonine residue on
CC       the protein receptor, but instead requires the prior addition of a
CC       GalNAc on a peptide before adding additional GalNAc moieties. Some
CC       peptide transferase activity is however not excluded, considering that
CC       its appropriate peptide substrate may remain unidentified.
CC       {ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450}.
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         Evidence={ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
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         Evidence={ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:10544240, ECO:0000305|PubMed:11925450}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in uterus, retina,
CC       kidney, small intestine, omentum, stomach and CNS.
CC       {ECO:0000269|PubMed:10544240}.
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=N-acetylgalactosaminyltransferase 7;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_489";
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DR   EMBL; AJ002744; CAB60270.1; -; mRNA.
DR   EMBL; AK075488; BAG52155.1; -; mRNA.
DR   EMBL; CH471056; EAX04761.1; -; Genomic_DNA.
DR   EMBL; BC035303; AAH35303.1; -; mRNA.
DR   EMBL; BC046129; AAH46129.1; -; mRNA.
DR   EMBL; BC047468; AAH47468.1; -; mRNA.
DR   CCDS; CCDS3815.1; -.
DR   RefSeq; NP_059119.2; NM_017423.2.
DR   PDB; 6IWQ; X-ray; 2.95 A; A/B/C/D/E/F=61-657.
DR   PDB; 6IWR; X-ray; 2.60 A; A/B/C/D/E/F=61-657.
DR   PDBsum; 6IWQ; -.
DR   PDBsum; 6IWR; -.
DR   AlphaFoldDB; Q86SF2; -.
DR   SMR; Q86SF2; -.
DR   BioGRID; 119735; 58.
DR   IntAct; Q86SF2; 22.
DR   MINT; Q86SF2; -.
DR   STRING; 9606.ENSP00000265000; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   UniLectin; Q86SF2; -.
DR   GlyGen; Q86SF2; 1 site, 2 O-linked glycans (1 site).
DR   iPTMnet; Q86SF2; -.
DR   PhosphoSitePlus; Q86SF2; -.
DR   SwissPalm; Q86SF2; -.
DR   BioMuta; GALNT7; -.
DR   DMDM; 51315961; -.
DR   EPD; Q86SF2; -.
DR   jPOST; Q86SF2; -.
DR   MassIVE; Q86SF2; -.
DR   MaxQB; Q86SF2; -.
DR   PaxDb; 9606-ENSP00000265000; -.
DR   PeptideAtlas; Q86SF2; -.
DR   ProteomicsDB; 69579; -.
DR   Pumba; Q86SF2; -.
DR   Antibodypedia; 28517; 121 antibodies from 24 providers.
DR   DNASU; 51809; -.
DR   Ensembl; ENST00000265000.9; ENSP00000265000.4; ENSG00000109586.12.
DR   GeneID; 51809; -.
DR   KEGG; hsa:51809; -.
DR   MANE-Select; ENST00000265000.9; ENSP00000265000.4; NM_017423.3; NP_059119.2.
DR   UCSC; uc003isz.4; human.
DR   AGR; HGNC:4129; -.
DR   CTD; 51809; -.
DR   DisGeNET; 51809; -.
DR   GeneCards; GALNT7; -.
DR   HGNC; HGNC:4129; GALNT7.
DR   HPA; ENSG00000109586; Tissue enhanced (stomach).
DR   MIM; 605005; gene.
DR   neXtProt; NX_Q86SF2; -.
DR   OpenTargets; ENSG00000109586; -.
DR   PharmGKB; PA28542; -.
DR   VEuPathDB; HostDB:ENSG00000109586; -.
DR   eggNOG; KOG3737; Eukaryota.
DR   GeneTree; ENSGT00940000158105; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q86SF2; -.
DR   OMA; MNNIHTV; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q86SF2; -.
DR   TreeFam; TF352176; -.
DR   BRENDA; 2.4.1.41; 2681.
DR   PathwayCommons; Q86SF2; -.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   SignaLink; Q86SF2; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 51809; 11 hits in 1157 CRISPR screens.
DR   ChiTaRS; GALNT7; human.
DR   GenomeRNAi; 51809; -.
DR   Pharos; Q86SF2; Tbio.
DR   PRO; PR:Q86SF2; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q86SF2; Protein.
DR   Bgee; ENSG00000109586; Expressed in mucosa of sigmoid colon and 201 other cell types or tissues.
DR   ExpressionAtlas; Q86SF2; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
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:SF68; N-ACETYLGALACTOSAMINYLTRANSFERASE 7; 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.
DR   Genevisible; Q86SF2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycosyltransferase; Golgi apparatus; Lectin;
KW   Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..657
FT                   /note="N-acetylgalactosaminyltransferase 7"
FT                   /id="PRO_0000059116"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..657
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          532..652
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          31..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..317
FT                   /note="Catalytic subdomain A"
FT   REGION          381..443
FT                   /note="Catalytic subdomain B"
FT   COMPBIAS        36..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        197..435
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        426..507
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        545..562
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        585..600
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        625..640
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   CONFLICT        188
FT                   /note="S -> N (in Ref. 1; CAB60270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="F -> C (in Ref. 1; CAB60270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="G -> S (in Ref. 1; CAB60270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="K -> Q (in Ref. 1; CAB60270)"
FT                   /evidence="ECO:0000305"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           177..182
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           195..199
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          209..217
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           220..233
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           236..238
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          239..246
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           257..261
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          268..273
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           279..290
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           311..320
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          324..334
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          352..356
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          362..366
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           369..373
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          376..380
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          389..395
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           396..402
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           415..425
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          429..442
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           460..472
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           474..476
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           477..483
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           485..487
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           496..504
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           510..516
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           521..523
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          531..539
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          542..547
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          558..561
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           567..569
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          571..574
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          579..581
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          584..589
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   TURN            590..593
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          594..599
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          608..611
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   TURN            612..615
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          616..622
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          625..628
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          630..632
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          634..638
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   HELIX           645..647
FT                   /evidence="ECO:0007829|PDB:6IWR"
FT   STRAND          649..652
FT                   /evidence="ECO:0007829|PDB:6IWR"
SQ   SEQUENCE   657 AA;  75389 MW;  D78CB5CBDA4B02FA CRC64;
     MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP MPNRGGNGLA
     PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG GDSQKDIMQR QYLTFKPQTF
     TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG EKAKPLVLGP EFKQAIQASI KEFGFNMVAS
     DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA
     EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
     DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG YARGAWDWSM
     LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF ELGLYDPGLQ IWGGENFEIS
     YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF
     YASRPESQAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF
     ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC
     NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE MNNIHSV
//