ID   SPB5_MOUSE              Reviewed;         375 AA.
AC   P70124; Q3ULZ0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Serpin B5;
DE   AltName: Full=Maspin;
DE   AltName: Full=Peptidase inhibitor 5;
DE            Short=PI-5;
GN   Name=Serpinb5; Synonyms=Pi5, Spi5, Spi7;
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].
RX   PubMed=9132279; DOI=10.1007/bf03401667;
RA   Zhang M., Sheng S., Maass N., Sager R.;
RT   "mMaspin: the mouse homolog of a human tumor suppressor gene inhibits
RT   mammary tumor invasion and motility.";
RL   Mol. Med. 3:49-59(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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: Tumor suppressor. It blocks the growth, invasion, and
CC       metastatic properties of mammary tumors. As it does not undergo the S
CC       (stressed) to R (relaxed) conformational transition characteristic of
CC       active serpins, it exhibits no serine protease inhibitory activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with IRF6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U54705; AAB06042.1; -; mRNA.
DR   EMBL; AK136532; BAE23032.1; -; mRNA.
DR   EMBL; AK145220; BAE26308.1; -; mRNA.
DR   EMBL; CH466520; EDL39856.1; -; Genomic_DNA.
DR   EMBL; CH466520; EDL39857.1; -; Genomic_DNA.
DR   EMBL; BC005434; AAH05434.1; -; mRNA.
DR   CCDS; CCDS35684.1; -.
DR   RefSeq; NP_033283.1; NM_009257.3.
DR   AlphaFoldDB; P70124; -.
DR   SMR; P70124; -.
DR   BioGRID; 203447; 12.
DR   STRING; 10090.ENSMUSP00000108350; -.
DR   MEROPS; I04.980; -.
DR   GlyCosmos; P70124; 3 sites, No reported glycans.
DR   GlyGen; P70124; 3 sites.
DR   iPTMnet; P70124; -.
DR   PhosphoSitePlus; P70124; -.
DR   CPTAC; non-CPTAC-4010; -.
DR   EPD; P70124; -.
DR   MaxQB; P70124; -.
DR   PaxDb; 10090-ENSMUSP00000083908; -.
DR   PeptideAtlas; P70124; -.
DR   ProteomicsDB; 257340; -.
DR   Pumba; P70124; -.
DR   Antibodypedia; 4036; 650 antibodies from 43 providers.
DR   DNASU; 20724; -.
DR   Ensembl; ENSMUST00000086701.13; ENSMUSP00000083908.7; ENSMUSG00000067006.13.
DR   Ensembl; ENSMUST00000112729.3; ENSMUSP00000108349.2; ENSMUSG00000067006.13.
DR   Ensembl; ENSMUST00000112730.8; ENSMUSP00000108350.2; ENSMUSG00000067006.13.
DR   GeneID; 20724; -.
DR   KEGG; mmu:20724; -.
DR   UCSC; uc007cha.1; mouse.
DR   AGR; MGI:109579; -.
DR   CTD; 5268; -.
DR   MGI; MGI:109579; Serpinb5.
DR   VEuPathDB; HostDB:ENSMUSG00000067006; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000160674; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P70124; -.
DR   OMA; IFAPLCT; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P70124; -.
DR   TreeFam; TF352619; -.
DR   BioGRID-ORCS; 20724; 1 hit in 79 CRISPR screens.
DR   PRO; PR:P70124; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P70124; Protein.
DR   Bgee; ENSMUSG00000067006; Expressed in tail skin and 108 other cell types or tissues.
DR   ExpressionAtlas; P70124; baseline and differential.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR   GO; GO:0060512; P:prostate gland morphogenesis; IMP:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR   CDD; cd02057; serpinB5_maspin; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   InterPro; IPR000240; Serpin_B9/Maspin.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   InterPro; IPR033836; SERPINB5_serpin_dom.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF55; SERPIN B5; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00676; MASPIN.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P70124; MM.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted.
FT   CHAIN           1..375
FT                   /note="Serpin B5"
FT                   /id="PRO_0000032487"
FT   SITE            340..341
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  42111 MW;  5894DD8B9A76F9A7 CRC64;
     MDALRLANSA FAVDLFKQLC ERDPAGNILF SPICLSTSLS LAQVGTKGDT ANEIGQVLHF
     ENVKDVPFGF QTVTSDVNKL SSFYSLKLVK RLYIDKSLNP STEFISSTKR PYAKELETVD
     FKDKLEETKG QINSSIKELT DGHFEDILSE NSISDQTKIL VVNAAYFVGK WMKKFPESET
     KECPFRISKT DTKPVQMMNL EATFCLGNID DISCKIIELP FQNKHLSMLI VLPKDVEDES
     TGLEKIEQQL NPETLLQWTN PSTMANAKVK LSLPKFKVEK MIDPKASLES LGLKSLFNES
     TSDFSGMSET KGVSLSNVIH RVCLEITEDG GESIEVPGSR ILQHKDEFNA DHPFIYIIRH
     NKTRNIIFFG KFCSP
//