ENTK_HUMAN
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 03-AUG-2022, entry version 211.
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};
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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 PDBsum; 4DGJ; -.
DR PDBsum; 6ZOV; -.
DR AlphaFoldDB; P98073; -.
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 GlyGen; P98073; 18 sites.
DR iPTMnet; P98073; -.
DR PhosphoSitePlus; P98073; -.
DR BioMuta; TMPRSS15; -.
DR DMDM; 317373442; -.
DR MassIVE; P98073; -.
DR PaxDb; P98073; -.
DR PeptideAtlas; P98073; -.
DR PRIDE; P98073; -.
DR ProteomicsDB; 57784; -.
DR Antibodypedia; 2519; 236 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 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; PSQQCLQ; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P98073; -.
DR TreeFam; TF351678; -.
DR BRENDA; 3.4.21.9; 2681.
DR PathwayCommons; P98073; -.
DR SignaLink; P98073; -.
DR BioGRID-ORCS; 5651; 8 hits in 1067 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 tissues.
DR ExpressionAtlas; P98073; baseline and differential.
DR Genevisible; P98073; HS.
DR GO; GO:0005903; C:brush border; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 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 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; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR SUPFAM; SSF82671; SSF82671; 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.
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 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 954..957
FT /evidence="ECO:0007829|PDB:4DGJ"
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
