PEPC_HUMAN
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 03-AUG-2022, entry version 200.
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; P20142; -.
DR PeptideAtlas; P20142; -.
DR PRIDE; P20142; -.
DR ProteomicsDB; 53726; -. [P20142-1]
DR ProteomicsDB; 53727; -. [P20142-2]
DR Antibodypedia; 15914; 485 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 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; LSNNGYC; -.
DR OrthoDB; 1619495at2759; -.
DR PhylomeDB; P20142; -.
DR TreeFam; TF314990; -.
DR BRENDA; 3.4.23.3; 2681.
DR PathwayCommons; P20142; -.
DR SignaLink; P20142; -.
DR BioGRID-ORCS; 5225; 15 hits in 1068 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 103 other tissues.
DR ExpressionAtlas; P20142; baseline and differential.
DR Genevisible; P20142; HS.
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; TAS:ProtInc.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033735; Gastricsin.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR PANTHER; PTHR13683:SF292; PTHR13683:SF292; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
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
