SPIT1_MOUSE
ID SPIT1_MOUSE Reviewed; 507 AA.
AC Q9R097; Q99J04;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=11406276; DOI=10.1016/s0167-4781(01)00216-0;
RA Itoh H., Kataoka H., Meng J.Y., Hamasuna R., Kitamura N., Koono M.;
RT "Mouse hepatocyte growth factor activator inhibitor type 1 (HAI-1) and type
RT 2 (HAI-2)/placental bikunin genes and their promoters.";
RL Biochim. Biophys. Acta 1519:92-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-229.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Inhibitor of HGF activator. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HGFAC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: This inhibitor contains two inhibitory domains.
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DR EMBL; AF099018; AAF02490.1; -; mRNA.
DR EMBL; AL929318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27946.1; -; Genomic_DNA.
DR EMBL; BC005769; AAH05769.1; -; mRNA.
DR CCDS; CCDS16597.1; -.
DR RefSeq; NP_058603.2; NM_016907.3.
DR RefSeq; XP_006499125.1; XM_006499062.3.
DR AlphaFoldDB; Q9R097; -.
DR SMR; Q9R097; -.
DR STRING; 10090.ENSMUSP00000028783; -.
DR MEROPS; I02.007; -.
DR MEROPS; I02.008; -.
DR GlyGen; Q9R097; 2 sites.
DR iPTMnet; Q9R097; -.
DR PhosphoSitePlus; Q9R097; -.
DR CPTAC; non-CPTAC-3615; -.
DR MaxQB; Q9R097; -.
DR PaxDb; Q9R097; -.
DR PeptideAtlas; Q9R097; -.
DR PRIDE; Q9R097; -.
DR ProteomicsDB; 258725; -.
DR Antibodypedia; 1540; 460 antibodies from 33 providers.
DR DNASU; 20732; -.
DR Ensembl; ENSMUST00000028783; ENSMUSP00000028783; ENSMUSG00000027315.
DR Ensembl; ENSMUST00000110816; ENSMUSP00000106440; ENSMUSG00000027315.
DR Ensembl; ENSMUST00000110817; ENSMUSP00000106441; ENSMUSG00000027315.
DR GeneID; 20732; -.
DR KEGG; mmu:20732; -.
DR UCSC; uc008ltk.1; mouse.
DR CTD; 6692; -.
DR MGI; MGI:1338033; Spint1.
DR VEuPathDB; HostDB:ENSMUSG00000027315; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000161683; -.
DR HOGENOM; CLU_032314_1_0_1; -.
DR InParanoid; Q9R097; -.
DR OMA; ENTDWHL; -.
DR OrthoDB; 687721at2759; -.
DR PhylomeDB; Q9R097; -.
DR TreeFam; TF325867; -.
DR Reactome; R-MMU-6806942; MET Receptor Activation.
DR Reactome; R-MMU-8852405; Signaling by MST1.
DR BioGRID-ORCS; 20732; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Spint1; mouse.
DR PRO; PR:Q9R097; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R097; protein.
DR Bgee; ENSMUSG00000027315; Expressed in small intestine Peyer's patch and 160 other tissues.
DR Genevisible; Q9R097; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0060429; P:epithelium development; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
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 Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..507
FT /note="Kunitz-type protease inhibitor 1"
FT /id="PRO_0000016884"
FT DOMAIN 51..134
FT /note="MANSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT DOMAIN 244..294
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 312..348
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 369..419
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 254..255
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 379..380
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 244..294
FT /evidence="ECO:0000250"
FT DISULFID 253..277
FT /evidence="ECO:0000250"
FT DISULFID 269..290
FT /evidence="ECO:0000250"
FT DISULFID 320..338
FT /evidence="ECO:0000250"
FT DISULFID 332..347
FT /evidence="ECO:0000250"
FT DISULFID 369..419
FT /evidence="ECO:0000250"
FT DISULFID 378..402
FT /evidence="ECO:0000250"
FT DISULFID 394..415
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="G -> R (in Ref. 1; AAF02490)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="K -> M (in Ref. 1; AAF02490)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="C -> S (in Ref. 1; AAF02490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 56591 MW; F7F9CCF2693D1F8D CRC64;
MAGRRLARAS ISAVGVWLLC ALGLQATEAE LPSAPAELPG GAACLSRFTS GVPSFVLDTE
ASVSNGATFL GSPTARRGWD CVRSCCTTQN CNLALVELQP DGGEDAISAC FLMNCLYEQN
FVCKFAPKEG FINYLTQELY RSYRELRTRG FGGSRIPRIW MGIDLKVQLQ KPLVLNEADN
TDWHLLQGDS DVRVERKRPE EVELWGLKEG TYLFQLTRTD SDQPEETANL TITVLTAKQT
EDYCLASYKV GRCRGSFPRW YYDPKEQICK SFTFGGCLGN KNNYLREEEC MLACKDVQGI
SPKRHHPVCS GSCHATQFRC SNGCCIDGFL ECDDTPDCPD GSDEATCEKY TSGFDELQNI
HFLSDKGYCA ELPDTGFCKE NIPRWYYNPF SERCARFTYG GCYGNKNNFE EEQQCLESCR
GISKKDVFGL RREGSIPTVG SAEVAIAVFL VICIIVVLTI LGYCFFKNQR KEFHSPLHHP
PPTPASSTVS TTEDTEHLVY NHTTQPL
