ID   SPB5_RAT                Reviewed;         375 AA.
AC   P70564;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-NOV-2023, entry version 131.
DE   RecName: Full=Serpin B5;
DE   AltName: Full=Maspin;
DE   AltName: Full=Peptidase inhibitor 5;
DE            Short=PI-5;
GN   Name=Serpinb5; Synonyms=Pi5;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Vagina;
RX   PubMed=9065806; DOI=10.1016/s0304-3835(97)04600-4;
RA   Umekita Y., Hiipakka R.A., Liao S.;
RT   "Rat and human maspins: structures, metastatic suppressor activity and
RT   mutation in prostate cancer cells.";
RL   Cancer Lett. 113:87-93(1997).
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; U58857; AAB06043.1; -; mRNA.
DR   RefSeq; NP_476449.1; NM_057108.2.
DR   AlphaFoldDB; P70564; -.
DR   SMR; P70564; -.
DR   STRING; 10116.ENSRNOP00000003625; -.
DR   MEROPS; I04.980; -.
DR   GlyCosmos; P70564; 5 sites, No reported glycans.
DR   GlyGen; P70564; 5 sites.
DR   iPTMnet; P70564; -.
DR   PhosphoSitePlus; P70564; -.
DR   PaxDb; 10116-ENSRNOP00000003625; -.
DR   GeneID; 116589; -.
DR   KEGG; rno:116589; -.
DR   UCSC; RGD:69342; rat.
DR   AGR; RGD:69342; -.
DR   CTD; 5268; -.
DR   RGD; 69342; Serpinb5.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P70564; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P70564; -.
DR   PRO; PR:P70564; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016528; C:sarcoplasm; ISO:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; ISO:RGD.
DR   GO; GO:0060512; P:prostate gland morphogenesis; ISO:RGD.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:RGD.
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.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted.
FT   CHAIN           1..375
FT                   /note="Serpin B5"
FT                   /id="PRO_0000032488"
FT   SITE            340..341
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
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;  42063 MW;  E82C4EC6A0F2E482 CRC64;
     MDALRLANSA FAVELFKQLC EKEPAGNILF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF
     ENVKDVPFGF KPITSDVNKL SSFYSLKLIK RLYIDKSLNL STEFISSTKR PYANELETVD
     FKDKLEETKG QINSSIKELT DGHFEDILPE NSISDQTKIL VVNAAYFVGK WMKKFPESET
     KECPFRINKT DTKPVQMMNL EATFCLGNID DINCKIIELP FQNKHLSMLI VLPKDVEDES
     TGLEKIEKQL NPETLLQWTN PSTMANAKVK LSLPKFKVEK MIDPKASLES LGLKSLFNES
     TSDFSGMSET KGVSVSNVIH RVCLEITEDG GDSIEVPGSR ILQHKDEFKA DHPFLFIVRH
     NKTRNIVFLG KFSSP
//