ST14_HUMAN
ID ST14_HUMAN Reviewed; 855 AA.
AC Q9Y5Y6; Q9BS01; Q9H3S0; Q9HB36; Q9HCA3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Suppressor of tumorigenicity 14 protein;
DE EC=3.4.21.109;
DE AltName: Full=Matriptase;
DE AltName: Full=Membrane-type serine protease 1;
DE Short=MT-SP1;
DE AltName: Full=Prostamin;
DE AltName: Full=Serine protease 14;
DE AltName: Full=Serine protease TADG-15;
DE AltName: Full=Tumor-associated differentially-expressed gene 15 protein;
GN Name=ST14; Synonyms=PRSS14, SNC19, TADG15;
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].
RX PubMed=10373424; DOI=10.1074/jbc.274.26.18231;
RA Lin C.Y., Anders J., Johnson M., Sang Q.A., Dickson R.B.;
RT "Molecular cloning of cDNA for matriptase, a matrix-degrading serine
RT protease with trypsin-like activity.";
RL J. Biol. Chem. 274:18231-18236(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10500122; DOI=10.1073/pnas.96.20.11054;
RA Takeuchi T., Shuman M.A., Craik C.S.;
RT "Reverse biochemistry: use of macromolecular protease inhibitors to dissect
RT complex biological processes and identify a membrane-type serine protease
RT in epithelial cancer and normal tissue.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11054-11061(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RA Yamaguchi N., Mitsui S.;
RT "Molecular cloning of a novel transmembrane serine protease expressed in
RT human prostate.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-381.
RA Tanimoto H., Underwood L.J., Wang Y., Shigemasa K., Parmley T.H.,
RA O'Brien T.J.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Muscle;
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 [GENOMIC DNA] OF 340-664.
RA Cao J., Fan W., Zheng S.;
RT "Genomic analysis of a novel human serine protease SNC19.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION.
RC TISSUE=Milk;
RX PubMed=10373425; DOI=10.1074/jbc.274.26.18237;
RA Lin C.Y., Anders J., Johnson M., Dickson R.B.;
RT "Purification and characterization of a complex containing matriptase and a
RT Kunitz-type serine protease inhibitor from human milk.";
RL J. Biol. Chem. 274:18237-18242(1999).
RN [8]
RP INTERACTION WITH CDCP1.
RX PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL Oncogene 24:5333-5343(2005).
RN [9]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-656; ASP-711 AND SER-805, AND
RP POSSIBLE INTERACTION WITH TMEFF1.
RX PubMed=16407223; DOI=10.1074/jbc.m510687200;
RA Ge W., Hu H., Ding K., Sun L., Zheng S.;
RT "Protein interaction analysis of ST14 domains and their point and deletion
RT mutants.";
RL J. Biol. Chem. 281:7406-7412(2006).
RN [10]
RP FUNCTION, AND INVOLVEMENT IN ARCI11.
RX PubMed=18843291; DOI=10.1038/jid.2008.311;
RA Alef T., Torres S., Hausser I., Metze D., Tursen U., Lestringant G.G.,
RA Hennies H.C.;
RT "Ichthyosis, follicular atrophoderma, and hypotrichosis caused by mutations
RT in ST14 is associated with impaired profilaggrin processing.";
RL J. Invest. Dermatol. 129:862-869(2009).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 615-855 IN COMPLEX WITH
RP INHIBITORS, AND DISULFIDE BONDS.
RX PubMed=11696548; DOI=10.1074/jbc.m109830200;
RA Friedrich R., Fuentes-Prior P., Ong E., Coombs G., Hunter M., Oehler R.,
RA Pierson D., Gonzalez R., Huber R., Bode W., Madison E.L.;
RT "Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading
RT transmembrane serine proteinase.";
RL J. Biol. Chem. 277:2160-2168(2002).
RN [13]
RP VARIANT ARCI11 ARG-827.
RX PubMed=17273967; DOI=10.1086/512487;
RA Basel-Vanagaite L., Attia R., Ishida-Yamamoto A., Rainshtein L.,
RA Ben Amitai D., Lurie R., Pasmanik-Chor M., Indelman M., Zvulunov A.,
RA Saban S., Magal N., Sprecher E., Shohat M.;
RT "Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in
RT ST14, encoding type II transmembrane serine protease matriptase.";
RL Am. J. Hum. Genet. 80:467-477(2007).
CC -!- FUNCTION: Degrades extracellular matrix. Proposed to play a role in
CC breast cancer invasion and metastasis. Exhibits trypsin-like activity
CC as defined by cleavage of synthetic substrates with Arg or Lys as the
CC P1 site. Involved in the terminal differentiation of keratinocytes
CC through prostasin (PRSS8) activation and filaggrin (FLG) processing.
CC {ECO:0000269|PubMed:18843291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1
CC position and prefers small side-chain amino acids, such as Ala and
CC Gly, at the P2 position.; EC=3.4.21.109;
CC Evidence={ECO:0000269|PubMed:16407223};
CC -!- SUBUNIT: Interacts with CDCP1. May interact with TMEFF1.
CC {ECO:0000269|PubMed:11696548, ECO:0000269|PubMed:16007225}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 11 (ARCI11)
CC [MIM:602400]: A form of autosomal recessive congenital ichthyosis, a
CC disorder of keratinization with abnormal differentiation and
CC desquamation of the epidermis, resulting in abnormal skin scaling over
CC the whole body. The main skin phenotypes are lamellar ichthyosis (LI)
CC and non-bullous congenital ichthyosiform erythroderma (NCIE), although
CC phenotypic overlap within the same patient or among patients from the
CC same family can occur. Lamellar ichthyosis is a condition often
CC associated with an embedment in a collodion-like membrane at birth;
CC skin scales later develop, covering the entire body surface. Non-
CC bullous congenital ichthyosiform erythroderma characterized by fine
CC whitish scaling on an erythrodermal background; larger brownish scales
CC are present on the buttocks, neck and legs.
CC {ECO:0000269|PubMed:17273967, ECO:0000269|PubMed:18843291}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF118224; AAD42765.2; -; mRNA.
DR EMBL; AF133086; AAF00109.1; -; mRNA.
DR EMBL; AB030036; BAB20376.1; -; mRNA.
DR EMBL; AF057145; AAG15395.1; -; mRNA.
DR EMBL; BC005826; AAH05826.2; -; mRNA.
DR EMBL; BC030532; AAH30532.1; -; mRNA.
DR EMBL; AF283256; AAG13949.1; -; Genomic_DNA.
DR CCDS; CCDS8487.1; -.
DR RefSeq; NP_068813.1; NM_021978.3.
DR PDB; 1EAW; X-ray; 2.93 A; A/C=615-855.
DR PDB; 1EAX; X-ray; 1.30 A; A=615-855.
DR PDB; 2GV6; X-ray; 2.10 A; A=615-855.
DR PDB; 2GV7; X-ray; 2.20 A; A=615-855.
DR PDB; 3BN9; X-ray; 2.17 A; A/B=615-855.
DR PDB; 3NCL; X-ray; 1.19 A; A=615-855.
DR PDB; 3NPS; X-ray; 1.50 A; A=615-855.
DR PDB; 3P8F; X-ray; 2.00 A; A=615-855.
DR PDB; 3P8G; X-ray; 1.20 A; A=615-855.
DR PDB; 3SO3; X-ray; 2.10 A; A=615-855.
DR PDB; 4IS5; X-ray; 1.48 A; A=615-855.
DR PDB; 4ISL; X-ray; 2.29 A; A=615-855.
DR PDB; 4ISN; X-ray; 2.45 A; A=615-855.
DR PDB; 4ISO; X-ray; 2.01 A; A=615-855.
DR PDB; 4JYT; X-ray; 2.00 A; A=615-855.
DR PDB; 4JZ1; X-ray; 1.90 A; A=615-855.
DR PDB; 4JZI; X-ray; 2.00 A; A=615-855.
DR PDB; 4O97; X-ray; 2.20 A; A=615-855, B=604-607.
DR PDB; 4O9V; X-ray; 1.90 A; A=615-855, B=604-607.
DR PDB; 4R0I; X-ray; 1.90 A; A=615-855.
DR PDB; 5LYO; X-ray; 2.50 A; A/B/C=604-855.
DR PDB; 6N4T; X-ray; 1.95 A; A=615-855.
DR PDB; 6T9T; X-ray; 1.69 A; A=615-855.
DR PDBsum; 1EAW; -.
DR PDBsum; 1EAX; -.
DR PDBsum; 2GV6; -.
DR PDBsum; 2GV7; -.
DR PDBsum; 3BN9; -.
DR PDBsum; 3NCL; -.
DR PDBsum; 3NPS; -.
DR PDBsum; 3P8F; -.
DR PDBsum; 3P8G; -.
DR PDBsum; 3SO3; -.
DR PDBsum; 4IS5; -.
DR PDBsum; 4ISL; -.
DR PDBsum; 4ISN; -.
DR PDBsum; 4ISO; -.
DR PDBsum; 4JYT; -.
DR PDBsum; 4JZ1; -.
DR PDBsum; 4JZI; -.
DR PDBsum; 4O97; -.
DR PDBsum; 4O9V; -.
DR PDBsum; 4R0I; -.
DR PDBsum; 5LYO; -.
DR PDBsum; 6N4T; -.
DR PDBsum; 6T9T; -.
DR AlphaFoldDB; Q9Y5Y6; -.
DR SMR; Q9Y5Y6; -.
DR BioGRID; 112645; 286.
DR IntAct; Q9Y5Y6; 17.
DR MINT; Q9Y5Y6; -.
DR STRING; 9606.ENSP00000278742; -.
DR BindingDB; Q9Y5Y6; -.
DR ChEMBL; CHEMBL3018; -.
DR DrugBank; DB03127; Benzamidine.
DR DrugBank; DB13729; Camostat.
DR DrugBank; DB00013; Urokinase.
DR DrugCentral; Q9Y5Y6; -.
DR GuidetoPHARMACOLOGY; 2418; -.
DR MEROPS; S01.302; -.
DR TCDB; 8.A.131.1.4; the transmembrane protease serine 3 (tmprss3) family.
DR GlyConnect; 1779; 8 N-Linked glycans (3 sites).
DR GlyGen; Q9Y5Y6; 11 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; Q9Y5Y6; -.
DR PhosphoSitePlus; Q9Y5Y6; -.
DR BioMuta; ST14; -.
DR DMDM; 13124575; -.
DR EPD; Q9Y5Y6; -.
DR jPOST; Q9Y5Y6; -.
DR MassIVE; Q9Y5Y6; -.
DR MaxQB; Q9Y5Y6; -.
DR PaxDb; Q9Y5Y6; -.
DR PeptideAtlas; Q9Y5Y6; -.
DR PRIDE; Q9Y5Y6; -.
DR ProteomicsDB; 86543; -.
DR ABCD; Q9Y5Y6; 3 sequenced antibodies.
DR Antibodypedia; 33087; 406 antibodies from 36 providers.
DR DNASU; 6768; -.
DR Ensembl; ENST00000278742.6; ENSP00000278742.5; ENSG00000149418.11.
DR GeneID; 6768; -.
DR KEGG; hsa:6768; -.
DR MANE-Select; ENST00000278742.6; ENSP00000278742.5; NM_021978.4; NP_068813.1.
DR UCSC; uc001qfw.4; human.
DR CTD; 6768; -.
DR DisGeNET; 6768; -.
DR GeneCards; ST14; -.
DR HGNC; HGNC:11344; ST14.
DR HPA; ENSG00000149418; Tissue enhanced (intestine).
DR MalaCards; ST14; -.
DR MIM; 602400; phenotype.
DR MIM; 606797; gene.
DR neXtProt; NX_Q9Y5Y6; -.
DR OpenTargets; ENSG00000149418; -.
DR Orphanet; 91132; Ichthyosis-hypotrichosis syndrome.
DR PharmGKB; PA36168; -.
DR VEuPathDB; HostDB:ENSG00000149418; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155418; -.
DR HOGENOM; CLU_006842_19_3_1; -.
DR InParanoid; Q9Y5Y6; -.
DR OMA; CTWDIQV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9Y5Y6; -.
DR TreeFam; TF330647; -.
DR BRENDA; 3.4.21.109; 2681.
DR PathwayCommons; Q9Y5Y6; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q9Y5Y6; -.
DR BioGRID-ORCS; 6768; 18 hits in 1073 CRISPR screens.
DR ChiTaRS; ST14; human.
DR EvolutionaryTrace; Q9Y5Y6; -.
DR GenomeRNAi; 6768; -.
DR Pharos; Q9Y5Y6; Tchem.
DR PRO; PR:Q9Y5Y6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y5Y6; protein.
DR Bgee; ENSG00000149418; Expressed in mucosa of transverse colon and 173 other tissues.
DR Genevisible; Q9Y5Y6; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0060672; P:epithelial cell morphogenesis involved in placental branching; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR Gene3D; 4.10.400.10; -; 4.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR017051; Peptidase_S1A_matripase.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_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; 4.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036370; ST14; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57424; SSF57424; 4.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50024; SEA; 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; Disease variant; Disulfide bond; Glycoprotein; Hydrolase;
KW Hypotrichosis; Ichthyosis; Membrane; Protease; Reference proteome; Repeat;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..855
FT /note="Suppressor of tumorigenicity 14 protein"
FT /id="PRO_0000088712"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 86..203
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 214..334
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 340..447
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 452..487
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 487..524
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 524..560
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 566..603
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 615..854
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 656
FT /note="Charge relay system"
FT ACT_SITE 711
FT /note="Charge relay system"
FT ACT_SITE 805
FT /note="Charge relay system"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..244
FT /evidence="ECO:0000250"
FT DISULFID 340..366
FT /evidence="ECO:0000250"
FT DISULFID 397..410
FT /evidence="ECO:0000250"
FT DISULFID 453..464
FT /evidence="ECO:0000250"
FT DISULFID 459..477
FT /evidence="ECO:0000250"
FT DISULFID 471..486
FT /evidence="ECO:0000250"
FT DISULFID 488..501
FT /evidence="ECO:0000250"
FT DISULFID 496..514
FT /evidence="ECO:0000250"
FT DISULFID 508..523
FT /evidence="ECO:0000250"
FT DISULFID 525..537
FT /evidence="ECO:0000250"
FT DISULFID 532..550
FT /evidence="ECO:0000250"
FT DISULFID 544..559
FT /evidence="ECO:0000250"
FT DISULFID 567..579
FT /evidence="ECO:0000250"
FT DISULFID 574..593
FT /evidence="ECO:0000250"
FT DISULFID 587..602
FT /evidence="ECO:0000250"
FT DISULFID 641..657
FT /evidence="ECO:0000269|PubMed:11696548"
FT DISULFID 776..790
FT /evidence="ECO:0000269|PubMed:11696548"
FT DISULFID 801..830
FT /evidence="ECO:0000269|PubMed:11696548"
FT VARIANT 285
FT /note="M -> I (in dbSNP:rs7126904)"
FT /id="VAR_032847"
FT VARIANT 381
FT /note="R -> S (in dbSNP:rs17667603)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_032848"
FT VARIANT 827
FT /note="G -> R (in ARCI11; dbSNP:rs137852931)"
FT /evidence="ECO:0000269|PubMed:17273967"
FT /id="VAR_032849"
FT MUTAGEN 656
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:16407223"
FT MUTAGEN 711
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:16407223"
FT MUTAGEN 805
FT /note="S->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:16407223"
FT CONFLICT 674
FT /note="A -> V (in Ref. 3; BAB20376)"
FT /evidence="ECO:0000305"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:3NCL"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 647..653
FT /evidence="ECO:0007829|PDB:3NCL"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:3NCL"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 683..688
FT /evidence="ECO:0007829|PDB:5LYO"
FT STRAND 690..699
FT /evidence="ECO:0007829|PDB:3NCL"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:3NPS"
FT STRAND 744..754
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 764..770
FT /evidence="ECO:0007829|PDB:3NCL"
FT HELIX 773..779
FT /evidence="ECO:0007829|PDB:3NCL"
FT TURN 781..783
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:3NCL"
FT TURN 802..806
FT /evidence="ECO:0007829|PDB:4JZ1"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:5LYO"
FT STRAND 818..826
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:3NCL"
FT STRAND 833..835
FT /evidence="ECO:0007829|PDB:5LYO"
FT STRAND 837..842
FT /evidence="ECO:0007829|PDB:3NCL"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:3NCL"
FT HELIX 846..853
FT /evidence="ECO:0007829|PDB:3NCL"
SQ SEQUENCE 855 AA; 94770 MW; 26143132C01F99C9 CRC64;
MGSDRARKGG GGPKDFGAGL KYNSRHEKVN GLEEGVEFLP VNNVKKVEKH GPGRWVVLAA
VLIGLLLVLL GIGFLVWHLQ YRDVRVQKVF NGYMRITNEN FVDAYENSNS TEFVSLASKV
KDALKLLYSG VPFLGPYHKE SAVTAFSEGS VIAYYWSEFS IPQHLVEEAE RVMAEERVVM
LPPRARSLKS FVVTSVVAFP TDSKTVQRTQ DNSCSFGLHA RGVELMRFTT PGFPDSPYPA
HARCQWALRG DADSVLSLTF RSFDLASCDE RGSDLVTVYN TLSPMEPHAL VQLCGTYPPS
YNLTFHSSQN VLLITLITNT ERRHPGFEAT FFQLPRMSSC GGRLRKAQGT FNSPYYPGHY
PPNIDCTWNI EVPNNQHVKV RFKFFYLLEP GVPAGTCPKD YVEINGEKYC GERSQFVVTS
NSNKITVRFH SDQSYTDTGF LAEYLSYDSS DPCPGQFTCR TGRCIRKELR CDGWADCTDH
SDELNCSCDA GHQFTCKNKF CKPLFWVCDS VNDCGDNSDE QGCSCPAQTF RCSNGKCLSK
SQQCNGKDDC GDGSDEASCP KVNVVTCTKH TYRCLNGLCL SKGNPECDGK EDCSDGSDEK
DCDCGLRSFT RQARVVGGTD ADEGEWPWQV SLHALGQGHI CGASLISPNW LVSAAHCYID
DRGFRYSDPT QWTAFLGLHD QSQRSAPGVQ ERRLKRIISH PFFNDFTFDY DIALLELEKP
AEYSSMVRPI CLPDASHVFP AGKAIWVTGW GHTQYGGTGA LILQKGEIRV INQTTCENLL
PQQITPRMMC VGFLSGGVDS CQGDSGGPLS SVEADGRIFQ AGVVSWGDGC AQRNKPGVYT
RLPLFRDWIK ENTGV
