SPIT2_MOUSE
ID SPIT2_MOUSE Reviewed; 252 AA.
AC Q9WU03; Q5D0F2; Q9WU04; Q9WU05;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Kunitz-type protease inhibitor 2;
DE AltName: Full=Hepatocyte growth factor activator inhibitor type 2;
DE Short=HAI-2;
DE Flags: Precursor;
GN Name=Spint2; Synonyms=Hai2;
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], AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=10049781; DOI=10.1006/bbrc.1999.0268;
RA Itoh H., Kataoka H., Hamasuna R., Kitamura N., Koono M.;
RT "Hepatocyte growth factor activator inhibitor type 2 lacking the first
RT Kunitz-type serine proteinase inhibitor domain is a predominant product in
RT mouse but not in human.";
RL Biochem. Biophys. Res. Commun. 255:740-748(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibitor of HGF activator.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9WU03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WU03-2; Sequence=VSP_003034;
CC Name=3;
CC IsoId=Q9WU03-3; Sequence=VSP_003034, VSP_003035, VSP_003036;
CC -!- TISSUE SPECIFICITY: Isoform 2 is more predominantly expressed than
CC isoform 1.
CC -!- DOMAIN: This inhibitor contains two inhibitory domains.
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DR EMBL; AF099016; AAD22172.1; -; mRNA.
DR EMBL; AF099019; AAD22173.1; -; mRNA.
DR EMBL; AF099020; AAD22174.1; -; mRNA.
DR EMBL; BC003431; AAH03431.1; -; mRNA.
DR EMBL; BC026419; AAH26419.1; -; mRNA.
DR CCDS; CCDS39869.1; -. [Q9WU03-2]
DR CCDS; CCDS39870.1; -. [Q9WU03-1]
DR PIR; JG0185; JG0185.
DR RefSeq; NP_001076017.1; NM_001082548.1. [Q9WU03-2]
DR RefSeq; NP_035594.1; NM_011464.2. [Q9WU03-1]
DR AlphaFoldDB; Q9WU03; -.
DR SMR; Q9WU03; -.
DR STRING; 10090.ENSMUSP00000096204; -.
DR MEROPS; I02.009; -.
DR MEROPS; I02.010; -.
DR GlyGen; Q9WU03; 2 sites.
DR iPTMnet; Q9WU03; -.
DR PhosphoSitePlus; Q9WU03; -.
DR SwissPalm; Q9WU03; -.
DR EPD; Q9WU03; -.
DR MaxQB; Q9WU03; -.
DR PaxDb; Q9WU03; -.
DR PRIDE; Q9WU03; -.
DR ProteomicsDB; 261620; -. [Q9WU03-1]
DR ProteomicsDB; 261621; -. [Q9WU03-2]
DR Antibodypedia; 2598; 399 antibodies from 33 providers.
DR DNASU; 20733; -.
DR Ensembl; ENSMUST00000098604; ENSMUSP00000096204; ENSMUSG00000074227. [Q9WU03-1]
DR Ensembl; ENSMUST00000108236; ENSMUSP00000103871; ENSMUSG00000074227. [Q9WU03-2]
DR Ensembl; ENSMUST00000207601; ENSMUSP00000146580; ENSMUSG00000074227. [Q9WU03-3]
DR GeneID; 20733; -.
DR KEGG; mmu:20733; -.
DR UCSC; uc009gbk.1; mouse. [Q9WU03-1]
DR UCSC; uc009gbl.1; mouse. [Q9WU03-2]
DR CTD; 10653; -.
DR MGI; MGI:1338031; Spint2.
DR VEuPathDB; HostDB:ENSMUSG00000074227; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000160348; -.
DR HOGENOM; CLU_1274754_0_0_1; -.
DR InParanoid; Q9WU03; -.
DR OMA; KEECMHR; -.
DR PhylomeDB; Q9WU03; -.
DR TreeFam; TF326553; -.
DR Reactome; R-MMU-6806942; MET Receptor Activation.
DR Reactome; R-MMU-8852405; Signaling by MST1.
DR BioGRID-ORCS; 20733; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Spint2; mouse.
DR PRO; PR:Q9WU03; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9WU03; protein.
DR Bgee; ENSMUSG00000074227; Expressed in small intestine Peyer's patch and 239 other tissues.
DR Genevisible; Q9WU03; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0060672; P:epithelial cell morphogenesis involved in placental branching; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:2000146; P:negative regulation of cell motility; ISO:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR CDD; cd00109; KU; 2.
DR Gene3D; 4.10.410.10; -; 2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; SSF57362; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Protease inhibitor; Reference proteome; Repeat; Serine protease inhibitor;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..252
FT /note="Kunitz-type protease inhibitor 2"
FT /id="PRO_0000016886"
FT TOPO_DOM 28..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..88
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 133..183
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 48..49
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 143..144
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 47..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 63..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 133..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 142..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 158..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT VAR_SEQ 37..93
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003034"
FT VAR_SEQ 114..128
FT /note="PRKQSAEDLSAEIFN -> CFVELSVAALFLFYA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003035"
FT VAR_SEQ 129..252
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003036"
SQ SEQUENCE 252 AA; 27914 MW; B2FF4B86924D4F8F CRC64;
MAQLCELRRG RALLALVASL LLSGAQVASR ELDVHESCGV SKVVGKCRAS IPRWWYNITD
GSCQPFVYGG CEGNGNNYQS KEECLDKCAG VTENTTDDMA RNRNGADSSV LSVPRKQSAE
DLSAEIFNYE EYCVPKAVTG PCRAAFPRWY YDTEKNSCIS FIYGGCRGNK NSYLSQEACM
QHCSGKQMHP FLTPGLKAVI LVGLFLMVLI LLLGTSMVCL IRVVRRKQER ALRTVWSTAD
DKEQLVKNTC VL
