ID   SPB5_PLEMO              Reviewed;         375 AA.
AC   B1MTB7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
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   Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC   Pitheciidae; Callicebinae; Plecturocebus.
OX   NCBI_TaxID=9523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA   Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA   Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA   Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA   Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA   Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA   Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA   Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA   Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA   Tsipouri V., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000624; ACA57862.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1MTB7; -.
DR   SMR; B1MTB7; -.
DR   MEROPS; I04.980; -.
DR   PRIDE; B1MTB7; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Glycoprotein; Secreted.
FT   CHAIN           1..375
FT                   /note="Serpin B5"
FT                   /id="PRO_0000372428"
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        155
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        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  42008 MW;  5BA76B7211DAD148 CRC64;
     MDALQLANSA FAVDMFKQLC EKEPVGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF
     ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD
     FKDKLEETKG QINNSIKDLT DGHFENILAD NSVSNQTKIL VVNAAYFVGK WMKKFPESET
     KECPFRVNKT DTKPVQMMNI EATFCMGNID SIDCKIIELP FQNKHLSMFI LLPKDVEDES
     TGLEKIEKQL NSEALAQWTN PSTMANAKVK LSIPKFKVEK IIDPKASLEN LGLKRIFSED
     TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFVYIIRH
     NKTRNIIFFG KFCSP