ID   D6RAR4_HUMAN            Unreviewed;       662 AA.
AC   D6RAR4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=HGF activator {ECO:0000313|Ensembl:ENSP00000421801.1};
GN   Name=HGFAC {ECO:0000313|Ensembl:ENSP00000421801.1};
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 {ECO:0000313|Ensembl:ENSP00000421801.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000421801.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000421801.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00479}.
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DR   EMBL; AL590235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001284368.1; NM_001297439.1.
DR   AlphaFoldDB; D6RAR4; -.
DR   SMR; D6RAR4; -.
DR   MassIVE; D6RAR4; -.
DR   PeptideAtlas; D6RAR4; -.
DR   ProteomicsDB; 13403; -.
DR   Antibodypedia; 3925; 199 antibodies from 23 providers.
DR   DNASU; 3083; -.
DR   Ensembl; ENST00000511533.1; ENSP00000421801.1; ENSG00000109758.9.
DR   GeneID; 3083; -.
DR   UCSC; uc010icw.4; human.
DR   CTD; 3083; -.
DR   HGNC; HGNC:4894; HGFAC.
DR   VEuPathDB; HostDB:ENSG00000109758; -.
DR   GeneTree; ENSGT00940000159778; -.
DR   HOGENOM; CLU_006842_18_1_1; -.
DR   OMA; ETRYEYF; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; D6RAR4; -.
DR   BioGRID-ORCS; 3083; 3 hits in 1145 CRISPR screens.
DR   ChiTaRS; HGFAC; human.
DR   GenomeRNAi; 3083; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000109758; Expressed in right lobe of liver and 89 other cell types or tissues.
DR   ExpressionAtlas; D6RAR4; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264:SF43; HEPATOCYTE GROWTH FACTOR ACTIVATOR; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001146; Factor_XII_HGFA; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00058; FN1; 1.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 1.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Proteomics identification {ECO:0007829|MaxQB:D6RAR4,
KW   ECO:0007829|PeptideAtlas:D6RAR4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..662
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003087349"
FT   DOMAIN          103..150
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          160..198
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          200..240
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          241..279
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          285..367
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          415..653
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          64..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        454
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT   ACT_SITE        504
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT   ACT_SITE        605
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT   DISULFID        169..186
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        250..267
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        269..278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   662 AA;  71483 MW;  F2A3D607370547F6 CRC64;
     MGRWAWVPSP WPPPGLGPFL LLLLLLLLLP RGFQPQPGGN RTESPEPNAT ATPAIPTILV
     TSVTSETPAT SAPEAEGPQS GGLPPPPRAV PSSSSPQAQA LTEDGRPCRF PFRYGGRMLH
     ACTSEGSAHR KWCATTHNYD RDRAWGYCVE ATPPPGGPAA LDPCASGPCL NGGSCSNTQD
     PQSYHCSCPR AFTGKDCGTE KCFDETRYEY LEGGDRWARV RQGHVEQCEC FGGRTWCEGT
     RHTACLSSPC LNGGTCHLIV ATGTTVCACP PGFAGRLCNI EPDERCFLGN GTGYRGVAST
     SASGLSCLAW NSDLLYQELH VDSVGAAALL GLGPHAYCRN PDNDERPWCY VVKDSALSWE
     YCRLEACDLE TEGRESLTRV QLSPDLLATL PEPASPGRQA CGRRHKKRTF LRPRIIGGSS
     SLPGSHPWLA AIYIGDSFCA GSLVHTCWVV SAAHCFSHSP PRDSVSVVLG QHFFNRTTDV
     TQTFGIEKYI PYTLYSVFNP SDHDLVLIRL KKKGDRCATR SQFVQPICLP EPGSTFPAGH
     KCQIAGWGHL DENVSGYSSS LREALVPLVA DHKCSSPEVY GADISPNMLC AGYFDCKSDA
     CQGDSGGPLA CEKNGVAYLY GIISWGDGCG RLHKPGVYTR VANYVDWIND RIRPPRRLVA
     PS
//