ID   SPB12_HUMAN             Reviewed;         405 AA.
AC   Q96P63; Q3SYB4;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Serpin B12;
GN   Name=SERPINB12;
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), FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11604408; DOI=10.1074/jbc.m108879200;
RA   Askew Y.S., Pak S.C., Luke C.J., Askew D.J., Cataltepe S., Mills D.R.,
RA   Kato H., Lehoczky J., Dewar K., Birren B., Silverman G.A.;
RT   "SERPINB12 is a novel member of the human ov-serpin family that is widely
RT   expressed and inhibits trypsin-like serine proteinases.";
RL   J. Biol. Chem. 276:49320-49330(2001).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [4]
RP   INTERACTION WITH SLFN12 AND USP14.
RX   PubMed=30045019; DOI=10.1159/000492019;
RA   Basson M.D., Wang Q., Chaturvedi L.S., More S., Vomhof-DeKrey E.E.,
RA   Al-Marsoummi S., Sun K., Kuhn L.A., Kovalenko P., Kiupel M.;
RT   "Schlafen 12 Interaction with SerpinB12 and Deubiquitylases Drives Human
RT   Enterocyte Differentiation.";
RL   Cell. Physiol. Biochem. 48:1274-1290(2018).
CC   -!- FUNCTION: Inhibits trypsin and plasmin, but not thrombin, coagulation
CC       factor Xa, or urokinase-type plasminogen activator (PubMed:11604408).
CC       May play a role in cell differentiation (PubMed:30045019).
CC       {ECO:0000269|PubMed:11604408, ECO:0000269|PubMed:30045019}.
CC   -!- SUBUNIT: Interacts with SLFN12; as part of a pathway regulating cell
CC       differentiation (PubMed:30045019). May interact with USP14
CC       (PubMed:30045019). {ECO:0000269|PubMed:30045019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96P63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96P63-2; Sequence=VSP_056279;
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain, bone
CC       marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and
CC       intestine. {ECO:0000269|PubMed:11604408}.
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; AF411191; AAL05571.1; -; mRNA.
DR   EMBL; AC090307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC103885; AAI03886.1; -; mRNA.
DR   CCDS; CCDS11984.1; -. [Q96P63-1]
DR   CCDS; CCDS77194.1; -. [Q96P63-2]
DR   RefSeq; NP_001294857.1; NM_001307928.1. [Q96P63-2]
DR   RefSeq; NP_536722.1; NM_080474.2. [Q96P63-1]
DR   RefSeq; XP_011524550.1; XM_011526248.1. [Q96P63-2]
DR   RefSeq; XP_011524551.1; XM_011526249.1. [Q96P63-2]
DR   RefSeq; XP_016881556.1; XM_017026067.1.
DR   AlphaFoldDB; Q96P63; -.
DR   SMR; Q96P63; -.
DR   BioGRID; 124597; 110.
DR   IntAct; Q96P63; 21.
DR   MINT; Q96P63; -.
DR   STRING; 9606.ENSP00000372218; -.
DR   MEROPS; I04.016; -.
DR   GlyGen; Q96P63; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96P63; -.
DR   PhosphoSitePlus; Q96P63; -.
DR   SwissPalm; Q96P63; -.
DR   BioMuta; SERPINB12; -.
DR   DMDM; 20140145; -.
DR   EPD; Q96P63; -.
DR   jPOST; Q96P63; -.
DR   MassIVE; Q96P63; -.
DR   MaxQB; Q96P63; -.
DR   PaxDb; 9606-ENSP00000269491; -.
DR   PeptideAtlas; Q96P63; -.
DR   ProteomicsDB; 61854; -.
DR   ProteomicsDB; 77637; -. [Q96P63-1]
DR   Antibodypedia; 10036; 236 antibodies from 23 providers.
DR   DNASU; 89777; -.
DR   Ensembl; ENST00000269491.6; ENSP00000269491.1; ENSG00000166634.7. [Q96P63-1]
DR   Ensembl; ENST00000382768.2; ENSP00000372218.1; ENSG00000166634.7. [Q96P63-2]
DR   GeneID; 89777; -.
DR   KEGG; hsa:89777; -.
DR   MANE-Select; ENST00000382768.2; ENSP00000372218.1; NM_001307928.2; NP_001294857.1. [Q96P63-2]
DR   UCSC; uc010xen.2; human. [Q96P63-1]
DR   AGR; HGNC:14220; -.
DR   CTD; 89777; -.
DR   DisGeNET; 89777; -.
DR   GeneCards; SERPINB12; -.
DR   HGNC; HGNC:14220; SERPINB12.
DR   HPA; ENSG00000166634; Tissue enhanced (cervix, skin, vagina).
DR   MIM; 615662; gene.
DR   neXtProt; NX_Q96P63; -.
DR   OpenTargets; ENSG00000166634; -.
DR   PharmGKB; PA37859; -.
DR   VEuPathDB; HostDB:ENSG00000166634; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161829; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q96P63; -.
DR   OMA; CYFGKLL; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q96P63; -.
DR   TreeFam; TF352619; -.
DR   PathwayCommons; Q96P63; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q96P63; -.
DR   BioGRID-ORCS; 89777; 11 hits in 1137 CRISPR screens.
DR   ChiTaRS; SERPINB12; human.
DR   GenomeRNAi; 89777; -.
DR   Pharos; Q96P63; Tbio.
DR   PRO; PR:Q96P63; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q96P63; Protein.
DR   Bgee; ENSG00000166634; Expressed in skin of leg and 41 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; NAS:UniProtKB.
DR   CDD; cd19571; serpinB12_yukopin; 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:SF125; SERPIN B12; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; Q96P63; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..405
FT                   /note="Serpin B12"
FT                   /id="PRO_0000094119"
FT   REGION          64..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            370..371
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         81
FT                   /note="K -> KVLADSSLEGQKKTTEPLDQQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056279"
FT   VARIANT         227
FT                   /note="K -> E (in dbSNP:rs35582068)"
FT                   /id="VAR_034513"
FT   VARIANT         289
FT                   /note="N -> T (in dbSNP:rs35352345)"
FT                   /id="VAR_034514"
FT   VARIANT         338
FT                   /note="N -> S (in dbSNP:rs11664907)"
FT                   /id="VAR_051952"
SQ   SEQUENCE   405 AA;  46276 MW;  FFE12D4C9B7F3DFA CRC64;
     MDSLVTANTK FCFDLFQEIG KDDRHKNIFF SPLSLSAALG MVRLGARSDS AHQIDEVLHF
     NEFSQNESKE PDPCLKSNKQ KAGSLNNESG LVSCYFGQLL SKLDRIKTDY TLSIANRLYG
     EQEFPICQEY LDGVIQFYHT TIESVDFQKN PEKSRQEINF WVECQSQGKI KELFSKDAIN
     AETVLVLVNA VYFKAKWETY FDHENTVDAP FCLNANENKS VKMMTQKGLY RIGFIEEVKA
     QILEMRYTKG KLSMFVLLPS HSKDNLKGLE ELERKITYEK MVAWSSSENM SEESVVLSFP
     RFTLEDSYDL NSILQDMGIT DIFDETRADL TGISPSPNLY LSKIIHKTFV EVDENGTQAA
     AATGAVVSER SLRSWVEFNA NHPFLFFIRH NKTQTILFYG RVCSP
//