SPB5_RAT
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 03-AUG-2022, entry version 127.
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 GlyGen; P70564; 5 sites.
DR iPTMnet; P70564; -.
DR PhosphoSitePlus; P70564; -.
DR PaxDb; P70564; -.
DR PRIDE; P70564; -.
DR GeneID; 116589; -.
DR KEGG; rno:116589; -.
DR UCSC; RGD:69342; rat.
DR CTD; 5268; -.
DR RGD; 69342; Serpinb5.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P70564; -.
DR OrthoDB; 1124079at2759; -.
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: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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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; -; 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 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