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Database: UniProt
Entry: Q9Y5Y6
LinkDB: Q9Y5Y6
Original site: Q9Y5Y6 
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   29-SEP-2021, entry version 209.
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; 2FMV; Model; -; A=214-447.
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; 2FMV; -.
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   SMR; Q9Y5Y6; -.
DR   BioGRID; 112645; 17.
DR   IntAct; Q9Y5Y6; 17.
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; 421 antibodies.
DR   DNASU; 6768; -.
DR   Ensembl; ENST00000278742; ENSP00000278742; ENSG00000149418.
DR   GeneID; 6768; -.
DR   KEGG; hsa:6768; -.
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; NQTTCEK; -.
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   BioGRID-ORCS; 6768; 9 hits in 1006 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 caecum and 224 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: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
//
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