ID ENTK_HUMAN Reviewed; 1019 AA. AC P98073; Q2NKL7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 220. DE RecName: Full=Enteropeptidase; DE EC=3.4.21.9; DE AltName: Full=Enterokinase; DE AltName: Full=Serine protease 7; DE AltName: Full=Transmembrane protease serine 15; DE Contains: DE RecName: Full=Enteropeptidase non-catalytic heavy chain; DE Contains: DE RecName: Full=Enteropeptidase catalytic light chain; DE Flags: Precursor; GN Name=TMPRSS15; Synonyms=ENTK, PRSS7; 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 GLN-134 AND SER-732. RC TISSUE=Duodenum; RX PubMed=7718557; DOI=10.1021/bi00014a008; RA Kitamoto Y., Veile R.A., Donis-Keller H., Sadler J.E.; RT "cDNA sequence and chromosomal localization of human enterokinase, the RT proteolytic activator of trypsinogen."; RL Biochemistry 34:4562-4568(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-134 AND SER-732, AND RP INVOLVEMENT IN ENTKD. RX PubMed=11719902; DOI=10.1086/338456; RA Holzinger A., Maier E.M., Buck C., Mayerhofer P.U., Kappler M., RA Haworth J.C., Moroz S.P., Hadorn H.-B., Sadler J.E., Roscher A.A.; RT "Mutations in the proenteropeptidase gene are the molecular cause of RT congenital enteropeptidase deficiency."; RL Am. J. Hum. Genet. 70:20-25(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-134 AND SER-732. 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 749-1019. RC TISSUE=Duodenum; RX PubMed=8052624; DOI=10.1073/pnas.91.16.7588; RA Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.; RT "Enterokinase, the initiator of intestinal digestion, is a mosaic protease RT composed of a distinctive assortment of domains."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 785-1019, AND DISULFIDE BONDS. RX PubMed=22488687; DOI=10.1002/prot.24084; RA Simeonov P., Zahn M., Strater N., Zuchner T.; RT "Crystal structure of a supercharged variant of the human enteropeptidase RT light chain."; RL Proteins 80:1907-1910(2012). CC -!- FUNCTION: Responsible for initiating activation of pancreatic CC proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). CC It catalyzes the conversion of trypsinogen to trypsin which in turn CC activates other proenzymes including chymotrypsinogen, CC procarboxypeptidases, and proelastases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Activation of trypsinogen by selective cleavage of 6-Lys-|- CC Ile-7 bond.; EC=3.4.21.9; CC -!- SUBUNIT: Heterodimer of a catalytic (light) chain and a multidomain CC (heavy) chain linked by a disulfide bond. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II CC membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Intestinal brush border. CC -!- PTM: The chains are derived from a single precursor that is cleaved by CC a trypsin-like protease. CC -!- DISEASE: Enterokinase deficiency (ENTKD) [MIM:226200]: Life-threatening CC intestinal malabsorption disorder characterized by diarrhea and failure CC to thrive. {ECO:0000269|PubMed:11719902}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB90389.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U09860; AAC50138.1; -; mRNA. DR EMBL; Y19124; CAB65555.1; -; Genomic_DNA. DR EMBL; Y19125; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19126; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19127; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19128; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19129; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19130; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19131; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19132; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19133; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19134; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19135; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19136; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19137; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19138; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19139; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19140; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19141; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19142; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19143; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; AL163217; CAB90389.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL163218; CAB90392.1; -; Genomic_DNA. DR EMBL; BC111749; AAI11750.1; -; mRNA. DR CCDS; CCDS13571.1; -. DR PIR; A56318; A56318. DR RefSeq; NP_002763.2; NM_002772.2. DR PDB; 4DGJ; X-ray; 1.90 A; A/B/C/D=785-1019. DR PDB; 6ZOV; X-ray; 2.19 A; A/B/C/D=785-1019. DR PDB; 7WQX; EM; 2.70 A; A=519-1019. DR PDBsum; 4DGJ; -. DR PDBsum; 6ZOV; -. DR PDBsum; 7WQX; -. DR AlphaFoldDB; P98073; -. DR EMDB; EMD-32714; -. DR EMDB; EMD-32715; -. DR EMDB; EMD-32716; -. DR EMDB; EMD-32717; -. DR SMR; P98073; -. DR BioGRID; 111632; 2. DR IntAct; P98073; 3. DR MINT; P98073; -. DR STRING; 9606.ENSP00000284885; -. DR BindingDB; P98073; -. DR ChEMBL; CHEMBL1741195; -. DR GuidetoPHARMACOLOGY; 3189; -. DR MEROPS; S01.156; -. DR GlyCosmos; P98073; 18 sites, No reported glycans. DR GlyGen; P98073; 18 sites. DR iPTMnet; P98073; -. DR PhosphoSitePlus; P98073; -. DR BioMuta; TMPRSS15; -. DR DMDM; 317373442; -. DR MassIVE; P98073; -. DR PaxDb; 9606-ENSP00000284885; -. DR PeptideAtlas; P98073; -. DR ProteomicsDB; 57784; -. DR Pumba; P98073; -. DR Antibodypedia; 2519; 257 antibodies from 29 providers. DR DNASU; 5651; -. DR Ensembl; ENST00000284885.8; ENSP00000284885.3; ENSG00000154646.9. DR GeneID; 5651; -. DR KEGG; hsa:5651; -. DR MANE-Select; ENST00000284885.8; ENSP00000284885.3; NM_002772.3; NP_002763.3. DR UCSC; uc002ykw.4; human. DR AGR; HGNC:9490; -. DR CTD; 5651; -. DR DisGeNET; 5651; -. DR GeneCards; TMPRSS15; -. DR HGNC; HGNC:9490; TMPRSS15. DR HPA; ENSG00000154646; Tissue enriched (intestine). DR MalaCards; TMPRSS15; -. DR MIM; 226200; phenotype. DR MIM; 606635; gene. DR neXtProt; NX_P98073; -. DR OpenTargets; ENSG00000154646; -. DR Orphanet; 168601; Congenital enteropathy due to enteropeptidase deficiency. DR PharmGKB; PA33839; -. DR VEuPathDB; HostDB:ENSG00000154646; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT00940000159353; -. DR HOGENOM; CLU_011803_0_0_1; -. DR InParanoid; P98073; -. DR OMA; THGICNG; -. DR OrthoDB; 4252799at2759; -. DR PhylomeDB; P98073; -. DR TreeFam; TF351678; -. DR BRENDA; 3.4.21.9; 2681. DR PathwayCommons; P98073; -. DR SignaLink; P98073; -. DR BioGRID-ORCS; 5651; 10 hits in 1144 CRISPR screens. DR ChiTaRS; TMPRSS15; human. DR GenomeRNAi; 5651; -. DR Pharos; P98073; Tchem. DR PRO; PR:P98073; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P98073; Protein. DR Bgee; ENSG00000154646; Expressed in jejunal mucosa and 40 other cell types or tissues. DR ExpressionAtlas; P98073; baseline and differential. DR GO; GO:0005903; C:brush border; TAS:ProtInc. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00041; CUB; 2. DR CDD; cd00112; LDLa; 2. DR CDD; cd06263; MAM; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2. DR Gene3D; 3.30.70.960; SEA domain; 1. DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2. DR Gene3D; 3.10.250.10; SRCR-like domain; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR036055; LDL_receptor-like_sf. DR InterPro; IPR023415; LDLR_class-A_CS. DR InterPro; IPR002172; LDrepeatLR_classA_rpt. DR InterPro; IPR000998; MAM_dom. DR InterPro; IPR011163; Pept_S1A_enterop. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR000082; SEA_dom. DR InterPro; IPR036364; SEA_dom_sf. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; SRCR-like_dom. DR InterPro; IPR036772; SRCR-like_dom_sf. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24252; ACROSIN-RELATED; 1. DR PANTHER; PTHR24252:SF15; TRANSMEMBRANE SERINE PROTEASE 15; 1. DR Pfam; PF00431; CUB; 2. DR Pfam; PF00057; Ldl_recept_a; 2. DR Pfam; PF00629; MAM; 1. DR Pfam; PF01390; SEA; 1. DR Pfam; PF15494; SRCR_2; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001138; Enteropeptidase; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00042; CUB; 2. DR SMART; SM00192; LDLa; 2. DR SMART; SM00137; MAM; 1. DR SMART; SM00200; SEA; 1. DR SMART; SM00202; SR; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57424; LDL receptor-like module; 2. DR SUPFAM; SSF82671; SEA domain; 1. DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2. DR SUPFAM; SSF56487; SRCR-like; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 2. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. DR PROSITE; PS50024; SEA; 1. DR PROSITE; PS50287; SRCR_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P98073; HS. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Lipoprotein; KW Membrane; Myristate; Protease; Reference proteome; Repeat; Serine protease; KW Signal-anchor; Transmembrane; Transmembrane helix; Zymogen. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..784 FT /note="Enteropeptidase non-catalytic heavy chain" FT /id="PRO_0000027719" FT CHAIN 785..1019 FT /note="Enteropeptidase catalytic light chain" FT /id="PRO_0000027720" FT TOPO_DOM 2..18 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 19..47 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 48..1019 FT /note="Extracellular" FT /evidence="ECO:0000255" FT DOMAIN 54..169 FT /note="SEA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT DOMAIN 182..223 FT /note="LDL-receptor class A 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 225..334 FT /note="CUB 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 342..504 FT /note="MAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128" FT DOMAIN 524..634 FT /note="CUB 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 641..679 FT /note="LDL-receptor class A 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 678..771 FT /note="SRCR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DOMAIN 785..1019 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 825 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 876 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 971 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 147 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 328 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 335 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 388 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 440 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 470 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 503 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 534 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 630 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 682 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 706 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 725 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 848 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 887 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 909 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 949 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 184..197 FT /evidence="ECO:0000250" FT DISULFID 191..210 FT /evidence="ECO:0000250" FT DISULFID 204..221 FT /evidence="ECO:0000250" FT DISULFID 225..253 FT /evidence="ECO:0000250" FT DISULFID 524..552 FT /evidence="ECO:0000250" FT DISULFID 643..655 FT /evidence="ECO:0000250" FT DISULFID 650..668 FT /evidence="ECO:0000250" FT DISULFID 662..677 FT /evidence="ECO:0000250" FT DISULFID 757..767 FT /evidence="ECO:0000250" FT DISULFID 772..896 FT /note="Interchain (between heavy and light chains)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059, FT ECO:0000255|PROSITE-ProRule:PRU00124, ECO:0000255|PROSITE- FT ProRule:PRU00196, ECO:0000255|PROSITE-ProRule:PRU00274" FT DISULFID 810..826 FT /evidence="ECO:0000269|PubMed:22488687" FT DISULFID 910..977 FT /evidence="ECO:0000269|PubMed:22488687" FT DISULFID 941..956 FT /evidence="ECO:0000269|PubMed:22488687" FT DISULFID 967..995 FT /evidence="ECO:0000269|PubMed:22488687" FT VARIANT 65 FT /note="T -> I (in dbSNP:rs35987974)" FT /id="VAR_031686" FT VARIANT 77 FT /note="K -> R (in dbSNP:rs2824804)" FT /id="VAR_021940" FT VARIANT 134 FT /note="E -> Q (in dbSNP:rs2824790)" FT /evidence="ECO:0000269|PubMed:11719902, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7718557" FT /id="VAR_031687" FT VARIANT 545 FT /note="S -> C (in dbSNP:rs8134187)" FT /id="VAR_031688" FT VARIANT 641 FT /note="E -> K (in dbSNP:rs2273204)" FT /id="VAR_020175" FT VARIANT 660 FT /note="N -> H (in dbSNP:rs11088674)" FT /id="VAR_024292" FT VARIANT 732 FT /note="P -> S (in dbSNP:rs2824721)" FT /evidence="ECO:0000269|PubMed:11719902, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7718557" FT /id="VAR_031689" FT VARIANT 828 FT /note="Y -> C (in dbSNP:rs8130110)" FT /id="VAR_031690" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:7WQX" FT TURN 540..543 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 551..553 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 555..557 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 563..572 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 578..583 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 586..589 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 598..600 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 608..617 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 626..636 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 647..649 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:7WQX" FT HELIX 658..660 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 661..665 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 668..670 FT /evidence="ECO:0007829|PDB:7WQX" FT TURN 672..674 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 693..695 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 698..700 FT /evidence="ECO:0007829|PDB:7WQX" FT HELIX 712..718 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 724..727 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 739..742 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 750..752 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 765..767 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 785..787 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 799..804 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 807..814 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 816..822 FT /evidence="ECO:0007829|PDB:4DGJ" FT HELIX 824..827 FT /evidence="ECO:0007829|PDB:4DGJ" FT HELIX 834..836 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 837..842 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 855..864 FT /evidence="ECO:0007829|PDB:4DGJ" FT TURN 870..873 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 878..884 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 909..919 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 929..936 FT /evidence="ECO:0007829|PDB:4DGJ" FT HELIX 938..944 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 946..948 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 954..957 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 962..964 FT /evidence="ECO:0007829|PDB:7WQX" FT STRAND 974..979 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 982..991 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 993..996 FT /evidence="ECO:0007829|PDB:4DGJ" FT STRAND 1002..1006 FT /evidence="ECO:0007829|PDB:4DGJ" FT HELIX 1007..1009 FT /evidence="ECO:0007829|PDB:4DGJ" FT HELIX 1011..1015 FT /evidence="ECO:0007829|PDB:4DGJ" SQ SEQUENCE 1019 AA; 112935 MW; 45288F0636E5EC52 CRC64; MGSKRGISSR HHSLSSYEIM FAALFAILVV LCAGLIAVSC LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDENVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIP EPCKADHFQC KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FPTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPKIVGGSN AKEGAWPWVV GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAI LGLHMKSNLT SPQTVPRLID EIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE NQVFPPGRNC SIAGWGTVVY QGTTANILQE ADVPLLSNER CQQQMPEYNI TENMICAGYE EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR PGVYARVSRF TEWIQSFLH //