GenomeNet

Database: UniProt
Entry: O43278
LinkDB: O43278
Original site: O43278 
ID   SPIT1_HUMAN             Reviewed;         529 AA.
AC   O43278; Q7Z7D2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   29-SEP-2021, entry version 199.
DE   RecName: Full=Kunitz-type protease inhibitor 1;
DE   AltName: Full=Hepatocyte growth factor activator inhibitor type 1;
DE            Short=HAI-1;
DE   Flags: Precursor;
GN   Name=SPINT1; Synonyms=HAI1; ORFNames=UNQ223/PRO256;
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] (ISOFORM 2).
RX   PubMed=9045658; DOI=10.1074/jbc.272.10.6370;
RA   Shimomura T., Denda K., Kitamura A., Kawaguchi T., Kito M., Kondo J.,
RA   Kagaya S., Qin L., Takata H., Miyazawa K., Kitamura N.;
RT   "Hepatocyte growth factor activator inhibitor, a novel Kunitz-type serine
RT   protease inhibitor.";
RL   J. Biol. Chem. 272:6370-6376(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kirchhofer D., Peek M., Li W., Stamos J., Eigenbrot C., Kadkhodayan S.,
RA   Eliott J.M., Corpuz R.T., Lazarus R.A., Moran P.;
RT   "Tissue-expression, protease-specificity and Kunitz domain functions of
RT   HAI-1B, a new splice variant of hepatocyte growth factor activator
RT   inhibitor-1.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon, and Placenta;
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   PARTIAL PROTEIN SEQUENCE, AND 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   [7]
RP   PROTEIN SEQUENCE OF 36-50.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 245-303 IN COMPLEX WITH HGFAC, AND
RP   DISULFIDE BONDS.
RX   PubMed=15713485; DOI=10.1016/j.jmb.2004.12.048;
RA   Shia S., Stamos J., Kirchhofer D., Fan B., Wu J., Corpuz R.T., Santell L.,
RA   Lazarus R.A., Eigenbrot C.;
RT   "Conformational lability in serine protease active sites: structures of
RT   hepatocyte growth factor activator (HGFA) alone and with the inhibitory
RT   domain from HGFA inhibitor-1B.";
RL   J. Mol. Biol. 346:1335-1349(2005).
CC   -!- FUNCTION: Inhibitor of HGF activator. Also acts as an inhibitor of
CC       matriptase (ST14).
CC   -!- SUBUNIT: Interacts with HGFAC. {ECO:0000269|PubMed:15713485}.
CC   -!- INTERACTION:
CC       O43278-2; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-12078338, EBI-10225815;
CC       O43278-2; Q8TD06: AGR3; NbExp=3; IntAct=EBI-12078338, EBI-3925742;
CC       O43278-2; O75508: CLDN11; NbExp=3; IntAct=EBI-12078338, EBI-12820543;
CC       O43278-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12078338, EBI-11989440;
CC       O43278-2; Q92520: FAM3C; NbExp=3; IntAct=EBI-12078338, EBI-2876774;
CC       O43278-2; P21145: MAL; NbExp=3; IntAct=EBI-12078338, EBI-3932027;
CC       O43278-2; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-12078338, EBI-10314552;
CC       O43278-2; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-12078338, EBI-8640191;
CC       O43278-2; P02787: TF; NbExp=3; IntAct=EBI-12078338, EBI-714319;
CC       O43278-2; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-12078338, EBI-1057733;
CC       O43278-2; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-12078338, EBI-10278423;
CC       O43278-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12078338, EBI-12111910;
CC       O43278-2; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-12078338, EBI-12045841;
CC       O43278-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12078338, EBI-947187;
CC       O43278-2; O75841: UPK1B; NbExp=3; IntAct=EBI-12078338, EBI-12237619;
CC       O43278-2; O95183: VAMP5; NbExp=3; IntAct=EBI-12078338, EBI-10191195;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=HAI-1B;
CC         IsoId=O43278-1; Sequence=Displayed;
CC       Name=2; Synonyms=HAI-1A;
CC         IsoId=O43278-2; Sequence=VSP_013019;
CC   -!- DOMAIN: This inhibitor contains two inhibitory domains.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SPINT1ID44384ch15q15.html";
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DR   EMBL; AB000095; BAA25014.1; -; mRNA.
DR   EMBL; AY296715; AAP44001.1; -; mRNA.
DR   EMBL; AY358969; AAQ89328.1; -; mRNA.
DR   EMBL; BT007425; AAP36093.1; -; mRNA.
DR   EMBL; BC004140; AAH04140.1; -; mRNA.
DR   EMBL; BC018702; AAH18702.1; -; mRNA.
DR   CCDS; CCDS10067.1; -. [O43278-1]
DR   CCDS; CCDS45231.1; -. [O43278-2]
DR   RefSeq; NP_001027539.1; NM_001032367.1. [O43278-2]
DR   RefSeq; NP_003701.1; NM_003710.3. [O43278-2]
DR   RefSeq; NP_857593.1; NM_181642.2. [O43278-1]
DR   RefSeq; XP_006720720.1; XM_006720657.1. [O43278-1]
DR   PDB; 1YC0; X-ray; 2.60 A; I=245-303.
DR   PDB; 2MSX; NMR; -; A=47-152.
DR   PDB; 4ISL; X-ray; 2.29 A; B=245-304.
DR   PDB; 4ISN; X-ray; 2.45 A; B=245-307.
DR   PDB; 4ISO; X-ray; 2.01 A; B=245-304.
DR   PDB; 5EZD; X-ray; 2.10 A; A/B=168-303.
DR   PDB; 5H7V; X-ray; 3.82 A; A=36-457.
DR   PDBsum; 1YC0; -.
DR   PDBsum; 2MSX; -.
DR   PDBsum; 4ISL; -.
DR   PDBsum; 4ISN; -.
DR   PDBsum; 4ISO; -.
DR   PDBsum; 5EZD; -.
DR   PDBsum; 5H7V; -.
DR   BMRB; O43278; -.
DR   SMR; O43278; -.
DR   BioGRID; 112570; 25.
DR   DIP; DIP-37949N; -.
DR   IntAct; O43278; 23.
DR   STRING; 9606.ENSP00000342098; -.
DR   MEROPS; I02.007; -.
DR   GlyGen; O43278; 6 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; O43278; -.
DR   PhosphoSitePlus; O43278; -.
DR   SwissPalm; O43278; -.
DR   BioMuta; SPINT1; -.
DR   EPD; O43278; -.
DR   jPOST; O43278; -.
DR   MassIVE; O43278; -.
DR   MaxQB; O43278; -.
DR   PaxDb; O43278; -.
DR   PeptideAtlas; O43278; -.
DR   PRIDE; O43278; -.
DR   ProteomicsDB; 48846; -. [O43278-1]
DR   ProteomicsDB; 48847; -. [O43278-2]
DR   Antibodypedia; 1540; 444 antibodies.
DR   DNASU; 6692; -.
DR   Ensembl; ENST00000344051; ENSP00000342098; ENSG00000166145. [O43278-1]
DR   Ensembl; ENST00000562057; ENSP00000457076; ENSG00000166145. [O43278-2]
DR   GeneID; 6692; -.
DR   KEGG; hsa:6692; -.
DR   UCSC; uc001zna.4; human. [O43278-1]
DR   CTD; 6692; -.
DR   DisGeNET; 6692; -.
DR   GeneCards; SPINT1; -.
DR   HGNC; HGNC:11246; SPINT1.
DR   HPA; ENSG00000166145; Tissue enhanced (intestine).
DR   MIM; 605123; gene.
DR   neXtProt; NX_O43278; -.
DR   OpenTargets; ENSG00000166145; -.
DR   PharmGKB; PA36076; -.
DR   VEuPathDB; HostDB:ENSG00000166145; -.
DR   eggNOG; KOG4295; Eukaryota.
DR   GeneTree; ENSGT00940000161683; -.
DR   InParanoid; O43278; -.
DR   OMA; ENTDWHL; -.
DR   OrthoDB; 687721at2759; -.
DR   PhylomeDB; O43278; -.
DR   TreeFam; TF325867; -.
DR   PathwayCommons; O43278; -.
DR   Reactome; R-HSA-6806942; MET Receptor Activation.
DR   Reactome; R-HSA-8852405; Signaling by MST1.
DR   BioGRID-ORCS; 6692; 24 hits in 1017 CRISPR screens.
DR   ChiTaRS; SPINT1; human.
DR   EvolutionaryTrace; O43278; -.
DR   GeneWiki; SPINT1; -.
DR   GenomeRNAi; 6692; -.
DR   Pharos; O43278; Tbio.
DR   PRO; PR:O43278; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O43278; protein.
DR   Bgee; ENSG00000166145; Expressed in lower esophagus mucosa and 187 other tissues.
DR   ExpressionAtlas; O43278; baseline and differential.
DR   Genevisible; O43278; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR   GO; GO:0045687; P:positive regulation of glial cell differentiation; IEA:Ensembl.
DR   CDD; cd00109; KU; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 4.10.400.10; -; 1.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR013980; MANSC_dom.
DR   InterPro; IPR011106; MANSC_N.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR042482; Spint1.
DR   PANTHER; PTHR46750; PTHR46750; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF07502; MANEC; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00765; MANEC; 1.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50986; MANSC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Repeat; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           36..529
FT                   /note="Kunitz-type protease inhibitor 1"
FT                   /id="PRO_0000016883"
FT   DOMAIN          57..140
FT                   /note="MANSC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT   DOMAIN          250..300
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          334..370
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          391..441
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            260..261
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   SITE            401..402
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        250..300
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   DISULFID        259..283
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   DISULFID        275..296
FT                   /evidence="ECO:0000269|PubMed:15713485"
FT   DISULFID        335..347
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        354..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        391..441
FT                   /evidence="ECO:0000250"
FT   DISULFID        400..424
FT                   /evidence="ECO:0000250"
FT   DISULFID        416..437
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         306..321
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9045658"
FT                   /id="VSP_013019"
FT   VARIANT         123
FT                   /note="Y -> C (in dbSNP:rs11549915)"
FT                   /id="VAR_050065"
FT   VARIANT         142
FT                   /note="T -> R (in dbSNP:rs12323939)"
FT                   /id="VAR_050066"
FT   VARIANT         337
FT                   /note="P -> L (in dbSNP:rs7165897)"
FT                   /id="VAR_050067"
FT   CONFLICT        469
FT                   /note="A -> T (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   HELIX           84..93
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   HELIX           146..149
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:2MSX"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          190..196
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          209..212
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          215..222
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   STRAND          234..240
FT                   /evidence="ECO:0007829|PDB:5EZD"
FT   HELIX           246..250
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   STRAND          273..280
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   STRAND          290..292
FT                   /evidence="ECO:0007829|PDB:4ISO"
FT   HELIX           293..300
FT                   /evidence="ECO:0007829|PDB:4ISO"
SQ   SEQUENCE   529 AA;  58398 MW;  A87F286C23C73422 CRC64;
     MAPARTMARA RLAPAGIPAV ALWLLCTLGL QGTQAGPPPA PPGLPAGADC LNSFTAGVPG
     FVLDTNASVS NGATFLESPT VRRGWDCVRA CCTTQNCNLA LVELQPDRGE DAIAACFLIN
     CLYEQNFVCK FAPREGFINY LTREVYRSYR QLRTQGFGGS GIPKAWAGID LKVQPQEPLV
     LKDVENTDWR LLRGDTDVRV ERKDPNQVEL WGLKEGTYLF QLTVTSSDHP EDTANVTVTV
     LSTKQTEDYC LASNKVGRCR GSFPRWYYDP TEQICKSFVY GGCLGNKNNY LREEECILAC
     RGVQGGPLRG SSGAQATFPQ GPSMERRHPV CSGTCQPTQF RCSNGCCIDS FLECDDTPNC
     PDASDEAACE KYTSGFDELQ RIHFPSDKGH CVDLPDTGLC KESIPRWYYN PFSEHCARFT
     YGGCYGNKNN FEEEQQCLES CRGISKKDVF GLRREIPIPS TGSVEMAVAV FLVICIVVVV
     AILGYCFFKN QRKDFHGHHH HPPPTPASST VSTTEDTEHL VYNHTTRPL
//
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