ID   SPB13_HUMAN             Reviewed;         391 AA.
AC   Q9UIV8; A8K2Q8; Q3MII2; Q9HCX1; Q9UBW1; Q9UKG0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Serpin B13;
DE   AltName: Full=HaCaT UV-repressible serpin;
DE            Short=Hurpin;
DE   AltName: Full=Headpin;
DE   AltName: Full=Peptidase inhibitor 13;
DE            Short=PI-13;
DE   AltName: Full=Proteinase inhibitor 13;
GN   Name=SERPINB13; Synonyms=PI13;
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).
RC   TISSUE=Skin;
RX   PubMed=10512713; DOI=10.1006/jmbi.1999.3159;
RA   Abts H.F., Welss T., Mirmohammadsadegh A., Koehrer K., Michel G.,
RA   Ruzicka T.;
RT   "Cloning and characterization of hurpin (Protease Inhibitor 13): a new skin
RT   specific, UV-repressible serine proteinase inhibitor of the ovalbumin
RT   serpin family.";
RL   J. Mol. Biol. 293:29-39(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-293.
RX   PubMed=10527881; DOI=10.1006/bbrc.1999.1453;
RA   Spring P., Nakashima T., Frederick M., Henderson Y., Clayman G.;
RT   "Identification and cDNA cloning of headpin, a novel differentially
RT   expressed serpin that maps to chromosome 18q.";
RL   Biochem. Biophys. Res. Commun. 264:299-304(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=11004515; DOI=10.1016/s0167-4781(00)00100-7;
RA   Nakashima T., Pak S.C., Silverman G.A., Spring P.M., Frederick M.J.,
RA   Clayman G.L.;
RT   "Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a
RT   serpin which is down-regulated in head and neck cancer cells.";
RL   Biochim. Biophys. Acta 1492:441-446(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=11313015; DOI=10.1089/104454901300068924;
RA   Abts H.F., Welss T., Scheuring S., Scott F.L., Irving J.A., Michel G.,
RA   Bird P.I., Ruzicka T.;
RT   "Sequence, organization, chromosomal localization and alternative splicing
RT   of the human serine protease inhibitor gene hurpin (PI13), which is up-
RT   regulated in psoriasis.";
RL   DNA Cell Biol. 20:123-131(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-293.
RC   TISSUE=Tongue;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-293.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [8]
RP   IDENTIFICATION BY MASS 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: May play a role in the proliferation or differentiation of
CC       keratinocytes.
CC   -!- INTERACTION:
CC       Q9UIV8; Q15700: DLG2; NbExp=3; IntAct=EBI-3048588, EBI-80426;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UIV8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UIV8-2; Sequence=VSP_006058;
CC   -!- TISSUE SPECIFICITY: Skin specific.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ001696; CAA04935.2; -; mRNA.
DR   EMBL; AJ001697; CAA04936.2; -; mRNA.
DR   EMBL; AJ001698; CAA04937.1; -; mRNA.
DR   EMBL; AF169949; AAD55765.1; -; mRNA.
DR   EMBL; AF216854; AAF72879.1; -; Genomic_DNA.
DR   EMBL; AJ278717; CAC03569.1; -; Genomic_DNA.
DR   EMBL; AK290323; BAF83012.1; -; mRNA.
DR   EMBL; AK313486; BAG36269.1; -; mRNA.
DR   EMBL; CH471096; EAW63153.1; -; Genomic_DNA.
DR   EMBL; BC101821; AAI01822.1; -; mRNA.
DR   CCDS; CCDS11985.1; -. [Q9UIV8-1]
DR   PIR; JC7118; JC7118.
DR   RefSeq; NP_001294852.1; NM_001307923.1.
DR   RefSeq; NP_036529.1; NM_012397.3. [Q9UIV8-1]
DR   AlphaFoldDB; Q9UIV8; -.
DR   SMR; Q9UIV8; -.
DR   BioGRID; 111293; 127.
DR   IntAct; Q9UIV8; 24.
DR   STRING; 9606.ENSP00000269489; -.
DR   MEROPS; I04.017; -.
DR   iPTMnet; Q9UIV8; -.
DR   PhosphoSitePlus; Q9UIV8; -.
DR   BioMuta; SERPINB13; -.
DR   DMDM; 12643252; -.
DR   EPD; Q9UIV8; -.
DR   MassIVE; Q9UIV8; -.
DR   MaxQB; Q9UIV8; -.
DR   PaxDb; 9606-ENSP00000341584; -.
DR   PeptideAtlas; Q9UIV8; -.
DR   PRIDE; Q9UIV8; -.
DR   ProteomicsDB; 84570; -. [Q9UIV8-1]
DR   ProteomicsDB; 84571; -. [Q9UIV8-2]
DR   Pumba; Q9UIV8; -.
DR   Antibodypedia; 10046; 258 antibodies from 28 providers.
DR   DNASU; 5275; -.
DR   Ensembl; ENST00000344731.10; ENSP00000341584.6; ENSG00000197641.12. [Q9UIV8-1]
DR   GeneID; 5275; -.
DR   KEGG; hsa:5275; -.
DR   MANE-Select; ENST00000344731.10; ENSP00000341584.6; NM_012397.4; NP_036529.1.
DR   UCSC; uc002ljc.4; human. [Q9UIV8-1]
DR   AGR; HGNC:8944; -.
DR   DisGeNET; 5275; -.
DR   GeneCards; SERPINB13; -.
DR   HGNC; HGNC:8944; SERPINB13.
DR   HPA; ENSG00000197641; Tissue enhanced (cervix, esophagus, vagina).
DR   MIM; 604445; gene.
DR   neXtProt; NX_Q9UIV8; -.
DR   OpenTargets; ENSG00000197641; -.
DR   PharmGKB; PA35512; -.
DR   VEuPathDB; HostDB:ENSG00000197641; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000162214; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q9UIV8; -.
DR   OMA; IHHQFQK; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q9UIV8; -.
DR   TreeFam; TF352619; -.
DR   PathwayCommons; Q9UIV8; -.
DR   Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR   SignaLink; Q9UIV8; -.
DR   BioGRID-ORCS; 5275; 9 hits in 1148 CRISPR screens.
DR   ChiTaRS; SERPINB13; human.
DR   GeneWiki; SERPINB13; -.
DR   GenomeRNAi; 5275; -.
DR   Pharos; Q9UIV8; Tbio.
DR   PRO; PR:Q9UIV8; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q9UIV8; Protein.
DR   Bgee; ENSG00000197641; Expressed in tongue squamous epithelium and 111 other cell types or tissues.
DR   ExpressionAtlas; Q9UIV8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:1902173; P:negative regulation of keratinocyte apoptotic process; IMP:UniProtKB.
DR   GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB.
DR   GO; GO:0009411; P:response to UV; TAS:ProtInc.
DR   CDD; cd19572; serpinB13_headpin; 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; 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   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF161; SERPIN B13; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; Q9UIV8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..391
FT                   /note="Serpin B13"
FT                   /id="PRO_0000094121"
FT   SITE            356..357
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         206..257
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006058"
FT   VARIANT         293
FT                   /note="G -> S (in dbSNP:rs1020694)"
FT                   /evidence="ECO:0000269|PubMed:10527881,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.6"
FT                   /id="VAR_024356"
FT   CONFLICT        8
FT                   /note="S -> N (in Ref. 4; CAC03569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="Missing (in Ref. 1; CAA04937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="E -> Q (in Ref. 1; CAA04937)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   391 AA;  44276 MW;  2CA88558D4BC2B09 CRC64;
     MDSLGAVSTR LGFDLFKELK KTNDGNIFFS PVGILTAIGM VLLGTRGATA SQLEEVFHSE
     KETKSSRIKA EEKEVIENTE AVHQQFQKFL TEISKLTNDY ELNITNRLFG EKTYLFLQKY
     LDYVEKYYHA SLEPVDFVNA ADESRKKINS WVESKTNEKI KDLFPDGSIS SSTKLVLVNM
     VYFKGQWDRE FKKENTKEEK FWMNKSTSKS VQMMTQSHSF SFTFLEDLQA KILGIPYKNN
     DLSMFVLLPN DIDGLEKIID KISPEKLVEW TSPGHMEERK VNLHLPRFEV EDGYDLEAVL
     AAMGMGDAFS EHKADYSGMS SGSGLYAQKF LHSSFVAVTE EGTEAAAATG IGFTVTSAPG
     HENVHCNHPF LFFIRHNESN SILFFGRFSS P
//