GenomeNet

Database: UniProt
Entry: Q4V8Q2_RAT
LinkDB: Q4V8Q2_RAT
Original site: Q4V8Q2_RAT 
ID   Q4V8Q2_RAT              Unreviewed;       507 AA.
AC   Q4V8Q2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   SubName: Full=Serine peptidase inhibitor, Kunitz type 1 {ECO:0000313|Ensembl:ENSRNOP00000017223.3};
GN   Name=Spint1 {ECO:0000313|Ensembl:ENSRNOP00000017223.3,
GN   ECO:0000313|RGD:1303138};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000017223.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000017223.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017223.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000017223.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017223.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001004265.2; NM_001004265.2.
DR   RefSeq; XP_006234825.1; XM_006234763.2.
DR   RefSeq; XP_006234826.1; XM_006234764.2.
DR   AlphaFoldDB; Q4V8Q2; -.
DR   SMR; Q4V8Q2; -.
DR   STRING; 10116.ENSRNOP00000017223; -.
DR   MEROPS; I02.008; -.
DR   PhosphoSitePlus; Q4V8Q2; -.
DR   PaxDb; 10116-ENSRNOP00000017223; -.
DR   Ensembl; ENSRNOT00000017223.5; ENSRNOP00000017223.3; ENSRNOG00000012811.6.
DR   GeneID; 311331; -.
DR   KEGG; rno:311331; -.
DR   AGR; RGD:1303138; -.
DR   CTD; 6692; -.
DR   RGD; 1303138; Spint1.
DR   eggNOG; KOG4295; Eukaryota.
DR   GeneTree; ENSGT00940000161683; -.
DR   OMA; CDETLDC; -.
DR   OrthoDB; 2909633at2759; -.
DR   TreeFam; TF325867; -.
DR   Reactome; R-RNO-6806942; MET Receptor Activation.
DR   Reactome; R-RNO-8852405; Signaling by MST1.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000012811; Expressed in jejunum and 19 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:RGD.
DR   GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; ISO:RGD.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IEP:RGD.
DR   GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:RGD.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:0060674; P:placenta blood vessel development; ISO:RGD.
DR   GO; GO:0045687; P:positive regulation of glial cell differentiation; IMP:RGD.
DR   CDD; cd22623; Kunitz_HAI1_1-like; 1.
DR   CDD; cd22624; Kunitz_HAI1_2-like; 1.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 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   PANTHER; PTHR46750; KUNITZ-TYPE PROTEASE INHIBITOR 1; 1.
DR   PANTHER; PTHR46750:SF1; KUNITZ-TYPE PROTEASE INHIBITOR 1; 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; BPTI-like; 2.
DR   SUPFAM; SSF57424; LDL receptor-like module; 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   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..507
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014309450"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DISULFID        313..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        320..338
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        332..347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   507 AA;  56498 MW;  3824D1E70C513D7E CRC64;
     MAARRLAQAS ISTVCVWLLC ALGLQGTETE LPSAPPEFSG GAACLNRFTS GVPAFVLDTE
     ASVSNGATFL GSPTVHRGWD CVRACCTTQN CNLALVELQP DGGEDAISAC FLMNCLYEQN
     FVCKFAPKDG FINYLTQDLY NSYRELRTRG FGGSRIPRIW MGIDLKVQLQ KPLVLRDADN
     TDWHLLQGDQ DVSVKRNHPE EVELWGLKEG TYLFQLTRTD SDQLEETVNL TITVLTAEQT
     EDYCLASYKV GRCRGSFPRW YYDPKEQICK SFTFGGCLGN KNNYLREEEC MLACKDVKGI
     SPKRHHPVCT GSCHSTQFQC SNGCCIDGFL ECDDTPDCPD GSDEATCEKY SSGFDELQSI
     HFLSDKGYCA ELPDTGFCKE NIPRWYYNPF SERCARFTYG GCYGNKNNFE KEQQCLESCR
     GISKKDVFGL RRESSVPSAG SVEVAIAVLL AVCIIVVLTI LGYCFFKNQK KNFHSPLHQP
     PPTPASSTVS TTEDTEHLVY NHTTQPL
//
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