ID   PEPC_HUMAN              Reviewed;         388 AA.
AC   P20142; B4DVZ3; Q5T3D7; Q5T3D8;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Gastricsin;
DE            EC=3.4.23.3;
DE   AltName: Full=Pepsinogen C;
DE   Flags: Precursor;
GN   Name=PGC;
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 [GENOMIC DNA].
RX   PubMed=3335549; DOI=10.1016/s0021-9258(19)57314-8;
RA   Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.;
RT   "Primary structure of human pepsinogen C gene.";
RL   J. Biol. Chem. 263:1382-1385(1988).
RN   [2]
RP   ERRATUM OF PUBMED:3335549.
RA   Hayano T., Sogawa K., Ichihara Y., Fujii-Kuriyama Y., Takahashi K.;
RL   J. Biol. Chem. 263:14592-14592(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2909526; DOI=10.1016/s0021-9258(17)31268-1;
RA   Taggart R.T., Cass L.G., Mohandas T.K., Derby P., Barr P.J., Pals G.,
RA   Bell G.I.;
RT   "Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization
RT   to chromosome 6, and sequence homology with pepsinogen A.";
RL   J. Biol. Chem. 264:375-379(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=2567697; DOI=10.1016/0888-7543(89)90292-9;
RA   Pals G., Azuma T., Mohandas T.K., Bell G.I., Bacon J., Samloff I.M.,
RA   Walz D.A., Barr P.J., Taggart R.T.;
RT   "Human pepsinogen C (progastricsin) polymorphism: evidence for a single
RT   locus located at 6p21.1-pter.";
RL   Genomics 4:137-148(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Wong R.N.S., Tang J.;
RT   "cDNA sequence of human gastricsin.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Stomach;
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
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   [9]
RP   PROTEIN SEQUENCE OF 17-101.
RX   PubMed=2515193; DOI=10.1093/oxfordjournals.jbchem.a122952;
RA   Athauda S.B.P., Tanji M., Kageyama T., Takahashi K.;
RT   "A comparative study on the NH2-terminal amino acid sequences and some
RT   other properties of six isozymic forms of human pepsinogens and pepsins.";
RL   J. Biochem. 106:920-927(1989).
RN   [10]
RP   PROTEIN SEQUENCE OF 17-64.
RX   PubMed=6816595;
RA   Foltmann B., Jensen A.L.;
RT   "Human progastricsin. Analysis of intermediates during activation into
RT   gastricsin and determination of the amino acid sequence of the propart.";
RL   Eur. J. Biochem. 128:63-70(1982).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS).
RX   PubMed=7714902; DOI=10.1006/jmbi.1994.0154;
RA   Moore S.A., Sielecki A.R., Chernaia M.M., Tarasova N.I., James M.N.G.;
RT   "Crystal and molecular structures of human progastricsin at 1.62-A
RT   resolution.";
RL   J. Mol. Biol. 247:466-485(1995).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS).
RX   PubMed=9406551; DOI=10.1038/nsb1297-1010;
RA   Khan A.R., Cherney M.M., Tarasova N.I., James M.N.;
RT   "Structural characterization of activation 'intermediate 2' on the pathway
RT   to human gastricsin.";
RL   Nat. Struct. Biol. 4:1010-1015(1997).
CC   -!- FUNCTION: Hydrolyzes a variety of proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=More restricted specificity than pepsin A, but shows
CC         preferential cleavage at Tyr-|-Xaa bonds. High activity on
CC         hemoglobin.; EC=3.4.23.3;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P20142-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P20142-2; Sequence=VSP_042312;
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60062.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M18667; AAA60062.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M18659; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18660; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18661; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18662; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18663; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18664; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18665; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; M18666; AAA60062.1; JOINED; Genomic_DNA.
DR   EMBL; J04443; AAA60074.1; -; mRNA.
DR   EMBL; M23077; AAA60063.1; -; Genomic_DNA.
DR   EMBL; M23069; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23070; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23071; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23072; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23073; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23074; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; M23075; AAA60063.1; JOINED; Genomic_DNA.
DR   EMBL; U75272; AAB18273.1; -; mRNA.
DR   EMBL; AK301298; BAG62855.1; -; mRNA.
DR   EMBL; AL365205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC073740; AAH73740.1; -; mRNA.
DR   CCDS; CCDS4859.1; -. [P20142-1]
DR   CCDS; CCDS55000.1; -. [P20142-2]
DR   PIR; A29937; A29937.
DR   RefSeq; NP_001159896.1; NM_001166424.1. [P20142-2]
DR   RefSeq; NP_002621.1; NM_002630.3. [P20142-1]
DR   PDB; 1AVF; X-ray; 2.36 A; A/J=60-388, P/Q=17-42.
DR   PDB; 1HTR; X-ray; 1.62 A; B=60-388, P=17-59.
DR   PDBsum; 1AVF; -.
DR   PDBsum; 1HTR; -.
DR   AlphaFoldDB; P20142; -.
DR   SMR; P20142; -.
DR   BioGRID; 111246; 9.
DR   IntAct; P20142; 1.
DR   STRING; 9606.ENSP00000362116; -.
DR   BindingDB; P20142; -.
DR   ChEMBL; CHEMBL2136; -.
DR   GuidetoPHARMACOLOGY; 2391; -.
DR   MEROPS; A01.003; -.
DR   TCDB; 8.A.32.1.4; the Beta-amyloid cleaving enzyme (bace1) family.
DR   iPTMnet; P20142; -.
DR   PhosphoSitePlus; P20142; -.
DR   BioMuta; PGC; -.
DR   DMDM; 129796; -.
DR   jPOST; P20142; -.
DR   MassIVE; P20142; -.
DR   MaxQB; P20142; -.
DR   PaxDb; 9606-ENSP00000362116; -.
DR   PeptideAtlas; P20142; -.
DR   ProteomicsDB; 53726; -. [P20142-1]
DR   ProteomicsDB; 53727; -. [P20142-2]
DR   Antibodypedia; 15914; 535 antibodies from 29 providers.
DR   DNASU; 5225; -.
DR   Ensembl; ENST00000373025.7; ENSP00000362116.3; ENSG00000096088.16. [P20142-1]
DR   Ensembl; ENST00000425343.6; ENSP00000405094.2; ENSG00000096088.16. [P20142-2]
DR   GeneID; 5225; -.
DR   KEGG; hsa:5225; -.
DR   MANE-Select; ENST00000373025.7; ENSP00000362116.3; NM_002630.4; NP_002621.1.
DR   UCSC; uc003ora.3; human. [P20142-1]
DR   AGR; HGNC:8890; -.
DR   CTD; 5225; -.
DR   DisGeNET; 5225; -.
DR   GeneCards; PGC; -.
DR   HGNC; HGNC:8890; PGC.
DR   HPA; ENSG00000096088; Tissue enriched (stomach).
DR   MIM; 169740; gene.
DR   neXtProt; NX_P20142; -.
DR   OpenTargets; ENSG00000096088; -.
DR   PharmGKB; PA33228; -.
DR   VEuPathDB; HostDB:ENSG00000096088; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000160626; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; P20142; -.
DR   OMA; KWMVLAL; -.
DR   OrthoDB; 1120702at2759; -.
DR   PhylomeDB; P20142; -.
DR   TreeFam; TF314990; -.
DR   BRENDA; 3.4.23.3; 2681.
DR   PathwayCommons; P20142; -.
DR   SignaLink; P20142; -.
DR   BioGRID-ORCS; 5225; 16 hits in 1146 CRISPR screens.
DR   ChiTaRS; PGC; human.
DR   EvolutionaryTrace; P20142; -.
DR   GeneWiki; Gastricsin; -.
DR   GenomeRNAi; 5225; -.
DR   Pharos; P20142; Tchem.
DR   PRO; PR:P20142; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P20142; Protein.
DR   Bgee; ENSG00000096088; Expressed in pylorus and 104 other cell types or tissues.
DR   ExpressionAtlas; P20142; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0007586; P:digestion; TAS:ProtInc.
DR   GO; GO:0002803; P:positive regulation of antibacterial peptide production; IMP:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05477; gastricsin; 1.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF72; GASTRICSIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   Genevisible; P20142; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Aspartyl protease; Digestion;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:2515193,
FT                   ECO:0000269|PubMed:6816595"
FT   PROPEP          17..59
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026056"
FT   CHAIN           60..388
FT                   /note="Gastricsin"
FT                   /id="PRO_0000026057"
FT   DOMAIN          73..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        91
FT   ACT_SITE        276
FT   DISULFID        104..109
FT   DISULFID        267..271
FT   DISULFID        310..343
FT   VAR_SEQ         217..388
FT                   /note="QQGSSGGAVVFGGVDSSLYTGQIYWAPVTQELYWQIGIEEFLIGGQASGWCS
FT                   EGCQAIVDTGTSLLTVPQQYMSALLQATGAQEDEYGQFLVNCNSIQNLPSLTFIINGVE
FT                   FPLPPSSYILSNNGYCTVGVEPTYLSSQNGQPLWILGDVFLRSYYSVYDLGNNRVGFAT
FT                   AA -> LVLESSGLGPLLTPSRAAPPSSTLQLPEKPLEQTWNILTPFTKTLPVSNLSRK
FT                   VTSWAGVGIPVTCLPEAGSGGERRAECGLGVPTTRGPPRSQHHSGA (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042312"
FT   CONFLICT        40..41
FT                   /note="GE -> ED (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="W -> S (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           29..35
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           39..43
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           50..54
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          84..91
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          124..134
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          137..150
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          153..165
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           169..173
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:1AVF"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:1AVF"
FT   HELIX           195..201
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          205..214
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          219..229
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          235..244
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          251..254
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          256..259
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   TURN            266..269
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           286..288
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           289..296
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           310..315
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           332..335
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          343..350
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          360..363
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   HELIX           365..368
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          371..376
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   TURN            377..380
FT                   /evidence="ECO:0007829|PDB:1HTR"
FT   STRAND          381..387
FT                   /evidence="ECO:0007829|PDB:1HTR"
SQ   SEQUENCE   388 AA;  42426 MW;  F862DFDC1438BB92 CRC64;
     MKWMVVVLVC LQLLEAAVVK VPLKKFKSIR ETMKEKGLLG EFLRTHKYDP AWKYRFGDLS
     VTYEPMAYMD AAYFGEISIG TPPQNFLVLF DTGSSNLWVP SVYCQSQACT SHSRFNPSES
     STYSTNGQTF SLQYGSGSLT GFFGYDTLTV QSIQVPNQEF GLSENEPGTN FVYAQFDGIM
     GLAYPALSVD EATTAMQGMV QEGALTSPVF SVYLSNQQGS SGGAVVFGGV DSSLYTGQIY
     WAPVTQELYW QIGIEEFLIG GQASGWCSEG CQAIVDTGTS LLTVPQQYMS ALLQATGAQE
     DEYGQFLVNC NSIQNLPSLT FIINGVEFPL PPSSYILSNN GYCTVGVEPT YLSSQNGQPL
     WILGDVFLRS YYSVYDLGNN RVGFATAA
//