SPB5_MOUSE
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 03-AUG-2022, entry version 156.
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; 11.
DR STRING; 10090.ENSMUSP00000083908; -.
DR MEROPS; I04.980; -.
DR GlyGen; P70124; 3 sites.
DR iPTMnet; P70124; -.
DR PhosphoSitePlus; P70124; -.
DR CPTAC; non-CPTAC-4010; -.
DR EPD; P70124; -.
DR MaxQB; P70124; -.
DR PaxDb; P70124; -.
DR PeptideAtlas; P70124; -.
DR PRIDE; P70124; -.
DR ProteomicsDB; 257340; -.
DR Antibodypedia; 4036; 576 antibodies from 43 providers.
DR DNASU; 20724; -.
DR Ensembl; ENSMUST00000086701; ENSMUSP00000083908; ENSMUSG00000067006.
DR Ensembl; ENSMUST00000112729; ENSMUSP00000108349; ENSMUSG00000067006.
DR Ensembl; ENSMUST00000112730; ENSMUSP00000108350; ENSMUSG00000067006.
DR GeneID; 20724; -.
DR KEGG; mmu:20724; -.
DR UCSC; uc007cha.1; mouse.
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; FSEMCET; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P70124; -.
DR TreeFam; TF352619; -.
DR BioGRID-ORCS; 20724; 1 hit in 74 CRISPR screens.
DR PRO; PR:P70124; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P70124; protein.
DR Bgee; ENSMUSG00000067006; Expressed in tail skin and 107 other tissues.
DR ExpressionAtlas; P70124; baseline and differential.
DR Genevisible; P70124; MM.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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; -; 1.
DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR PRINTS; PR00676; MASPIN.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
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
