SPB5_HUMAN
ID SPB5_HUMAN Reviewed; 375 AA.
AC P36952; B2R6Y4; Q6N0B4; Q8WW89;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 192.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PRO-176 AND LEU-187.
RC TISSUE=Mammary gland;
RX PubMed=8290962; DOI=10.1126/science.8290962;
RA Zou Z., Anisowicz A., Hendrix M.J.C., Thor A., Neveu M., Sheng S.,
RA Rafidi K., Seftor E., Sager R.;
RT "Maspin, a serpin with tumor-suppressing activity in human mammary
RT epithelial cells.";
RL Science 263:526-529(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-176.
RC TISSUE=Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-176.
RC TISSUE=Prostate;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-375 (ISOFORM 1), AND VARIANT
RP VAL-319.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PROTEIN SEQUENCE OF 341-360, AND CHARACTERIZATION.
RX PubMed=7797587; DOI=10.1074/jbc.270.26.15832;
RA Pemberton P.A., Wong D.T., Gibson H.L., Kiefer M.C., Fitzpatrick P.A.,
RA Sager R., Barr P.J.;
RT "The tumor suppressor maspin does not undergo the stressed to relaxed
RT transition or inhibit trypsin-like serine proteases. Evidence that maspin
RT is not a protease inhibitory serpin.";
RL J. Biol. Chem. 270:15832-15837(1995).
RN [7]
RP INTERACTION WITH IRF6.
RX PubMed=16049006; DOI=10.1074/jbc.m503523200;
RA Bailey C.M., Khalkhali-Ellis Z., Kondo S., Margaryan N.V., Seftor R.E.B.,
RA Wheaton W.W., Amir S., Pins M.R., Schutte B.C., Hendrix M.J.C.;
RT "Mammary serine protease inhibitor (Maspin) binds directly to interferon
RT regulatory factor 6: identification of a novel serpin partnership.";
RL J. Biol. Chem. 280:34210-34217(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=15760906; DOI=10.1074/jbc.m412043200;
RA Law R.H., Irving J.A., Buckle A.M., Ruzyla K., Buzza M.,
RA Bashtannyk-Puhalovich T.A., Beddoe T.C., Nguyen K., Worrall D.M.,
RA Bottomley S.P., Bird P.I., Rossjohn J., Whisstock J.C.;
RT "The high resolution crystal structure of the human tumor suppressor maspin
RT reveals a novel conformational switch in the G-helix.";
RL J. Biol. Chem. 280:22356-22364(2005).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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.
CC -!- SUBUNIT: Interacts with IRF6. {ECO:0000269|PubMed:16049006}.
CC -!- INTERACTION:
CC P36952; Q9Y6M0: PRSS21; NbExp=7; IntAct=EBI-2371394, EBI-7054564;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36952-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36952-2; Sequence=VSP_037145, VSP_037146;
CC -!- TISSUE SPECIFICITY: Normal mammary epithelial cells.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SerpinB5ID42267.html";
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; U04313; AAA18957.1; -; mRNA.
DR EMBL; AK312765; BAG35631.1; -; mRNA.
DR EMBL; AC036176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020713; AAH20713.1; -; mRNA.
DR EMBL; BX640597; CAE45703.1; -; mRNA.
DR CCDS; CCDS32839.1; -. [P36952-1]
DR PIR; A36898; A36898.
DR RefSeq; NP_002630.2; NM_002639.4. [P36952-1]
DR PDB; 1WZ9; X-ray; 2.10 A; A/B=1-375.
DR PDB; 1XQG; X-ray; 3.10 A; A/B=1-375.
DR PDB; 1XQJ; X-ray; 3.10 A; A=1-375.
DR PDB; 1XU8; X-ray; 2.80 A; A/B=1-375.
DR PDBsum; 1WZ9; -.
DR PDBsum; 1XQG; -.
DR PDBsum; 1XQJ; -.
DR PDBsum; 1XU8; -.
DR AlphaFoldDB; P36952; -.
DR SMR; P36952; -.
DR BioGRID; 111286; 158.
DR IntAct; P36952; 54.
DR MINT; P36952; -.
DR STRING; 9606.ENSP00000372221; -.
DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR MEROPS; I04.980; -.
DR GlyGen; P36952; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P36952; -.
DR MetOSite; P36952; -.
DR PhosphoSitePlus; P36952; -.
DR BioMuta; SERPINB5; -.
DR DMDM; 229462757; -.
DR CPTAC; CPTAC-582; -.
DR CPTAC; CPTAC-583; -.
DR EPD; P36952; -.
DR jPOST; P36952; -.
DR MassIVE; P36952; -.
DR MaxQB; P36952; -.
DR PaxDb; P36952; -.
DR PeptideAtlas; P36952; -.
DR PRIDE; P36952; -.
DR ProteomicsDB; 55240; -. [P36952-1]
DR ProteomicsDB; 55241; -. [P36952-2]
DR TopDownProteomics; P36952-1; -. [P36952-1]
DR Antibodypedia; 4036; 576 antibodies from 43 providers.
DR DNASU; 5268; -.
DR Ensembl; ENST00000382771.9; ENSP00000372221.4; ENSG00000206075.14. [P36952-1]
DR Ensembl; ENST00000489441.5; ENSP00000467158.1; ENSG00000206075.14. [P36952-2]
DR GeneID; 5268; -.
DR KEGG; hsa:5268; -.
DR MANE-Select; ENST00000382771.9; ENSP00000372221.4; NM_002639.5; NP_002630.2.
DR UCSC; uc002liy.3; human. [P36952-1]
DR CTD; 5268; -.
DR DisGeNET; 5268; -.
DR GeneCards; SERPINB5; -.
DR HGNC; HGNC:8949; SERPINB5.
DR HPA; ENSG00000206075; Tissue enhanced (esophagus, skin, urinary bladder).
DR MIM; 154790; gene.
DR neXtProt; NX_P36952; -.
DR OpenTargets; ENSG00000206075; -.
DR PharmGKB; PA35515; -.
DR VEuPathDB; HostDB:ENSG00000206075; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000160674; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; P36952; -.
DR OMA; FSEMCET; -.
DR PhylomeDB; P36952; -.
DR TreeFam; TF352619; -.
DR PathwayCommons; P36952; -.
DR SignaLink; P36952; -.
DR SIGNOR; P36952; -.
DR BioGRID-ORCS; 5268; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; SERPINB5; human.
DR EvolutionaryTrace; P36952; -.
DR GeneWiki; Maspin; -.
DR GenomeRNAi; 5268; -.
DR Pharos; P36952; Tbio.
DR PRO; PR:P36952; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P36952; protein.
DR Bgee; ENSG00000206075; Expressed in skin of abdomen and 95 other tissues.
DR ExpressionAtlas; P36952; baseline and differential.
DR Genevisible; P36952; HS.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0060512; P:prostate gland morphogenesis; IEA:Ensembl.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Secreted.
FT CHAIN 1..375
FT /note="Serpin B5"
FT /id="PRO_0000032486"
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 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 190..231
FT /note="TDTKPVQMMNMEATFCMGNIDSINCKIIELPFQNKHLSMFIL -> VCGAAC
FT SSKRSPIIDVKNDRDRVGHKSIPMRNLRARPAKCLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037145"
FT VAR_SEQ 232..375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037146"
FT VARIANT 176
FT /note="S -> P (in dbSNP:rs2289519)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8290962,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_055223"
FT VARIANT 187
FT /note="V -> L (in dbSNP:rs2289520)"
FT /evidence="ECO:0000269|PubMed:8290962"
FT /id="VAR_055224"
FT VARIANT 319
FT /note="I -> V (in dbSNP:rs1455555)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_022115"
FT CONFLICT 66
FT /note="V -> I (in Ref. 1; AAA18957)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="K -> Q (in Ref. 5; CAE45703)"
FT /evidence="ECO:0000305"
FT HELIX 2..22
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1XQG"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1XQG"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 109..115
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 192..209
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:1WZ9"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:1XU8"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 315..326
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 337..341
FT /evidence="ECO:0007829|PDB:1XQG"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:1WZ9"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:1WZ9"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:1WZ9"
SQ SEQUENCE 375 AA; 42100 MW; 9F24E18505912804 CRC64;
MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF
ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD
FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFSESET
KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES
TGLEKIEKQL NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED
TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH
NKTRNIIFFG KFCSP
