CATH_HUMAN
ID CATH_HUMAN Reviewed; 335 AA.
AC P09668; B2RBK0; Q96NY6; Q9BUM7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Pro-cathepsin H;
DE Contains:
DE RecName: Full=Cathepsin H mini chain;
DE Contains:
DE RecName: Full=Cathepsin H;
DE EC=3.4.22.16;
DE Contains:
DE RecName: Full=Cathepsin H heavy chain;
DE Contains:
DE RecName: Full=Cathepsin H light chain;
DE Flags: Precursor;
GN Name=CTSH; Synonyms=CPSB;
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], AND VARIANTS SER-26 AND TYR-179.
RC TISSUE=Liver;
RX PubMed=2587265; DOI=10.1093/nar/17.22.9471;
RA Fuchs R., Gassen H.G.;
RT "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine
RT proteinase.";
RL Nucleic Acids Res. 17:9471-9471(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-179.
RX PubMed=11796715; DOI=10.1074/jbc.m109557200;
RA Waghray A., Keppler D., Sloane B.F., Schuger L., Chen Y.Q.;
RT "Analysis of a truncated form of cathepsin H in human prostate tumor
RT cells.";
RL J. Biol. Chem. 277:11533-11538(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-26.
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-26.
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 88-335, AND VARIANT TYR-179.
RC TISSUE=Kidney;
RX PubMed=2849458; DOI=10.1515/bchm3.1988.369.1.469;
RA Fuchs R., Machleidt W., Gassen H.G.;
RT "Molecular cloning and sequencing of a cDNA coding for mature human kidney
RT cathepsin H.";
RL Biol. Chem. Hoppe-Seyler 369:469-475(1988).
RN [7]
RP PROTEIN SEQUENCE OF 98-105 AND 114-335, AND GLYCOSYLATION AT ASN-101 AND
RP ASN-230.
RC TISSUE=Kidney;
RX PubMed=3342889; DOI=10.1016/0014-5793(88)80028-0;
RA Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
RT "Amino acid sequences of the human kidney cathepsins H and L.";
RL FEBS Lett. 228:341-345(1988).
RN [8]
RP PROTEIN SEQUENCE OF 99-105; 116-159 AND 294-335.
RA Machleidt W., Ritonja A., Popovic T., Kotnik M., Brzin J., Turk V.,
RA Machleidt I., Mueller-Esterl W.;
RT "Human cathepsins B, H and L: characterization by amino acid sequences and
RT some kinetics of inhibition by the kininogens.";
RL (In) Turk V. (eds.);
RL Cysteine proteinases and their inhibitors, pp.3-18, Walter de Gruyter,
RL Berlin and New York (1986).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-126.
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: Important for the overall degradation of proteins in
CC lysosomes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably,
CC cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
CC -!- SUBUNIT: Composed of a mini chain and a large chain. The large chain
CC may be split into heavy and light chain. All chains are held together
CC by disulfide bonds.
CC -!- INTERACTION:
CC P09668; Q86V38: ATN1; NbExp=3; IntAct=EBI-6189940, EBI-11954292;
CC P09668; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-6189940, EBI-356015;
CC P09668; Q92876: KLK6; NbExp=3; IntAct=EBI-6189940, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CTSHID40206ch15q25.html";
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DR EMBL; X16832; CAA34734.1; -; mRNA.
DR EMBL; AF426247; AAL23961.1; -; mRNA.
DR EMBL; AK314698; BAG37247.1; -; mRNA.
DR EMBL; AC011944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002479; AAH02479.1; -; mRNA.
DR EMBL; X07549; CAA30428.1; -; mRNA.
DR EMBL; X07549; CAA30429.1; -; mRNA.
DR CCDS; CCDS10308.1; -.
DR PIR; S12486; KHHUH.
DR RefSeq; NP_004381.2; NM_004390.4.
DR PDB; 6CZK; X-ray; 2.00 A; A=1-335.
DR PDB; 6CZS; X-ray; 1.66 A; A=1-335.
DR PDBsum; 6CZK; -.
DR PDBsum; 6CZS; -.
DR AlphaFoldDB; P09668; -.
DR SMR; P09668; -.
DR BioGRID; 107892; 83.
DR IntAct; P09668; 19.
DR STRING; 9606.ENSP00000220166; -.
DR BindingDB; P09668; -.
DR ChEMBL; CHEMBL2225; -.
DR DrugBank; DB08526; CARBOBENZYLOXY-(L)-LEUCINYL-(L)LEUCINYL METHOXYMETHYLKETONE.
DR DrugBank; DB04126; N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-Butane.
DR DrugBank; DB02140; N1-(1-Dimethylcarbamoyl-2-Phenyl-Ethyl)-2-Oxo-N4-(2-Pyridin-2-Yl-Ethyl)-Succinamide.
DR DrugBank; DB03120; p-Toluenesulfonic acid.
DR GuidetoPHARMACOLOGY; 2349; -.
DR MEROPS; C01.040; -.
DR GlyGen; P09668; 6 sites.
DR iPTMnet; P09668; -.
DR PhosphoSitePlus; P09668; -.
DR BioMuta; CTSH; -.
DR DMDM; 288558851; -.
DR EPD; P09668; -.
DR jPOST; P09668; -.
DR MassIVE; P09668; -.
DR MaxQB; P09668; -.
DR PaxDb; P09668; -.
DR PeptideAtlas; P09668; -.
DR PRIDE; P09668; -.
DR ProteomicsDB; 52262; -.
DR Antibodypedia; 1041; 405 antibodies from 35 providers.
DR DNASU; 1512; -.
DR Ensembl; ENST00000220166.10; ENSP00000220166.6; ENSG00000103811.18.
DR GeneID; 1512; -.
DR KEGG; hsa:1512; -.
DR MANE-Select; ENST00000220166.10; ENSP00000220166.6; NM_004390.5; NP_004381.2.
DR UCSC; uc021srk.2; human.
DR CTD; 1512; -.
DR DisGeNET; 1512; -.
DR GeneCards; CTSH; -.
DR HGNC; HGNC:2535; CTSH.
DR HPA; ENSG00000103811; Tissue enhanced (lung).
DR MalaCards; CTSH; -.
DR MIM; 116820; gene.
DR neXtProt; NX_P09668; -.
DR OpenTargets; ENSG00000103811; -.
DR Orphanet; 2073; Narcolepsy type 1.
DR PharmGKB; PA27033; -.
DR VEuPathDB; HostDB:ENSG00000103811; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000160227; -.
DR InParanoid; P09668; -.
DR OMA; AYNNFGC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P09668; -.
DR TreeFam; TF328985; -.
DR BRENDA; 3.4.22.16; 2681.
DR PathwayCommons; P09668; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P09668; -.
DR SignaLink; P09668; -.
DR SIGNOR; P09668; -.
DR BioGRID-ORCS; 1512; 23 hits in 1084 CRISPR screens.
DR ChiTaRS; CTSH; human.
DR GeneWiki; Cathepsin_H; -.
DR GenomeRNAi; 1512; -.
DR Pharos; P09668; Tchem.
DR PRO; PR:P09668; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P09668; protein.
DR Bgee; ENSG00000103811; Expressed in cranial nerve II and 199 other tissues.
DR ExpressionAtlas; P09668; baseline and differential.
DR Genevisible; P09668; HS.
DR GO; GO:0097208; C:alveolar lamellar body; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0097486; C:multivesicular body lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0030108; F:HLA-A specific activating MHC class I receptor activity; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEP:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; TAS:UniProtKB.
DR GO; GO:0010815; P:bradykinin catabolic process; IDA:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
DR GO; GO:0060448; P:dichotomous subdivision of terminal units involved in lung branching; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0002764; P:immune response-regulating signaling pathway; IDA:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:0001656; P:metanephros development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010813; P:neuropeptide catabolic process; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0043129; P:surfactant homeostasis; IDA:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Signal; Thiol protease;
KW Zymogen.
FT SIGNAL 1..22
FT PROPEP 23..97
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3342889"
FT /id="PRO_0000026206"
FT PEPTIDE 98..105
FT /note="Cathepsin H mini chain"
FT /id="PRO_0000026207"
FT PROPEP 106..115
FT /evidence="ECO:0000269|Ref.8"
FT /id="PRO_0000026208"
FT CHAIN 116..335
FT /note="Cathepsin H"
FT /id="PRO_0000026209"
FT CHAIN 116..292
FT /note="Cathepsin H heavy chain"
FT /id="PRO_0000026210"
FT CHAIN 293..335
FT /note="Cathepsin H light chain"
FT /id="PRO_0000026211"
FT ACT_SITE 141
FT /evidence="ECO:0000250"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3342889"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:3342889"
FT DISULFID 102..327
FT /evidence="ECO:0000250"
FT DISULFID 138..181
FT /evidence="ECO:0000250"
FT DISULFID 172..214
FT /evidence="ECO:0000250"
FT DISULFID 272..322
FT /evidence="ECO:0000250"
FT VARIANT 11
FT /note="G -> R (in dbSNP:rs2289702)"
FT /id="VAR_057038"
FT VARIANT 23
FT /note="A -> T (in dbSNP:rs35001431)"
FT /id="VAR_057039"
FT VARIANT 26
FT /note="C -> S (in dbSNP:rs1036938)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2587265"
FT /id="VAR_060368"
FT VARIANT 126
FT /note="G -> R (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036478"
FT VARIANT 179
FT /note="H -> Y (in dbSNP:rs1130856)"
FT /evidence="ECO:0000269|PubMed:11796715,
FT ECO:0000269|PubMed:2587265, ECO:0000269|PubMed:2849458"
FT /id="VAR_067717"
FT CONFLICT 306
FT /note="Q -> E (in Ref. 7; AA sequence and 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 48..69
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6CZS"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6CZS"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:6CZS"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6CZS"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:6CZS"
SQ SEQUENCE 335 AA; 37394 MW; E2CF3A5EEA59C1D1 CRC64;
MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE YHHRLQTFAS
NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ NCSATKSNYL RGTGPYPPSV
DWRKKGNFVS PVKNQGACGS CWTFSTTGAL ESAIAIATGK MLSLAEQQLV DCAQDFNNHG
CQGGLPSQAF EYILYNKGIM GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV
EAVALYNPVS FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV
