ID SPB11_HUMAN Reviewed; 392 AA. AC Q96P15; A8K9R0; Q5Q120; Q5Q121; Q5Q122; Q5Q123; Q6ISD3; Q96P13; Q96P14; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 02-JUN-2021, entry version 136. DE RecName: Full=Serpin B11; GN Name=SERPINB11; 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], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS RP GLU-51; THR-148; ALA-181; THR-181; TRP-188; THR-293 AND SER-303. RX PubMed=17562709; DOI=10.1074/jbc.m703182200; RA Askew D.J., Cataltepe S., Kumar V., Edwards C., Pace S.M., Howarth R.N., RA Pak S.C., Askew Y.S., Bromme D., Luke C.J., Whisstock J.C., Silverman G.A.; RT "SERPINB11 is a new noninhibitory intracellular serpin. Common single RT nucleotide polymorphisms in the scaffold impair conformational change."; RL J. Biol. Chem. 282:24948-24960(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-181. RC TISSUE=Trachea; 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], AND VARIANT GLU-51. 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], AND VARIANT THR-181. 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). CC -!- FUNCTION: Has no serine protease inhibitory activity, probably due to CC mutations in the scaffold impairing conformational change. CC {ECO:0000269|PubMed:17562709}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=SERPINB11a; CC IsoId=Q96P15-1; Sequence=Displayed; CC Name=2; Synonyms=SERPINB11e; CC IsoId=Q96P15-2; Sequence=VSP_040671; CC Name=3; Synonyms=SERPINB11g; CC IsoId=Q96P15-3; Sequence=VSP_040670; CC -!- TISSUE SPECIFICITY: Detected in a restricted number of tissues, CC including lung, placenta, prostate, and tonsil. CC {ECO:0000269|PubMed:17562709}. CC -!- POLYMORPHISM: According to some authors, 4 of the identified SERPIN11 CC transcripts contained coding sequences that could be distinguished by CC different combinations of single nucleotide polymorphisms (designated CC SERPINB11a, SERPINB11b, SERPINB11c, and SERPINB11d), and one contained CC a nonsense mutation introducing a premature stop codon in position 90 CC identified in the official genome sequence (SERPINB11f) CC (PubMed:17562709). The sequence displayed here corresponds to CC SERPINB11a. {ECO:0000269|PubMed:17562709}. CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily. CC {ECO:0000305}. CC -!- CAUTION: Mutations in the scaffold leading to either a stop codon CC instead of a Glu at position 90, an Arg instead of the well conserved CC Trp at position 188, or a Pro instead of Ser at position 303 lead to CC the loss of inhibitory activity. {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; AF419953; AAL16056.1; -; mRNA. DR EMBL; AF419954; AAL16057.1; -; mRNA. DR EMBL; AF419955; AAL16058.1; -; mRNA. DR EMBL; AY792323; AAV73920.1; -; mRNA. DR EMBL; AY792324; AAV73921.1; -; mRNA. DR EMBL; AY792325; AAV73922.1; -; mRNA. DR EMBL; AY792326; AAV73923.1; -; mRNA. DR EMBL; AK292775; BAF85464.1; -; mRNA. DR EMBL; AC069356; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069596; AAH69596.1; -; mRNA. DR CCDS; CCDS77196.1; -. [Q96P15-2] DR RefSeq; NP_001278207.1; NM_001291278.1. DR RefSeq; NP_536723.2; NM_080475.3. DR SMR; Q96P15; -. DR BioGRID; 124598; 10. DR STRING; 9606.ENSP00000441497; -. DR MEROPS; I04.956; -. DR iPTMnet; Q96P15; -. DR PhosphoSitePlus; Q96P15; -. DR BioMuta; SERPINB11; -. DR DMDM; 20140144; -. DR EPD; Q96P15; -. DR MassIVE; Q96P15; -. DR PeptideAtlas; Q96P15; -. DR PRIDE; Q96P15; -. DR ProteomicsDB; 77594; -. [Q96P15-1] DR ProteomicsDB; 77595; -. [Q96P15-2] DR ProteomicsDB; 77596; -. [Q96P15-3] DR Antibodypedia; 23130; 129 antibodies. DR DNASU; 89778; -. DR Ensembl; ENST00000382749; ENSP00000421854; ENSG00000206072. DR GeneID; 89778; -. DR KEGG; hsa:89778; -. DR UCSC; uc032hfq.2; human. [Q96P15-1] DR CTD; 89778; -. DR DisGeNET; 89778; -. DR GeneCards; SERPINB11; -. DR HGNC; HGNC:14221; SERPINB11. DR HPA; ENSG00000206072; Group enriched (esophagus, lymphoid tissue, prostate, tongue). DR MIM; 615682; gene. DR neXtProt; NX_Q96P15; -. DR PharmGKB; PA37860; -. DR VEuPathDB; HostDB:ENSG00000206072.12; -. DR eggNOG; KOG2392; Eukaryota. DR InParanoid; Q96P15; -. DR OrthoDB; 1124079at2759; -. DR PhylomeDB; Q96P15; -. DR PathwayCommons; Q96P15; -. DR BioGRID-ORCS; 89778; 1 hit in 143 CRISPR screens. DR ChiTaRS; SERPINB11; human. DR GenomeRNAi; 89778; -. DR Pharos; Q96P15; Tdark. DR PRO; PR:Q96P15; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q96P15; protein. DR Bgee; ENSG00000206072; Expressed in esophagus and 79 other tissues. DR ExpressionAtlas; Q96P15; baseline and differential. DR Genevisible; Q96P15; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central. DR Gene3D; 2.30.39.10; -; 1. DR Gene3D; 3.30.497.10; -; 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; PTHR11461; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; SSF56574; 1. DR PROSITE; PS00284; SERPIN; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Cytoplasm; Protease inhibitor; Reference proteome; KW Serine protease inhibitor. FT CHAIN 1..392 FT /note="Serpin B11" FT /id="PRO_0000094117" FT REGION 341..365 FT /note="RCL" FT /evidence="ECO:0000250" FT SITE 357..358 FT /note="Reactive bond" FT /evidence="ECO:0000250" FT VAR_SEQ 57..258 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_040670" FT VAR_SEQ 120..206 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_040671" FT VARIANT 51 FT /note="A -> E (in dbSNP:rs1395268)" FT /evidence="ECO:0000269|PubMed:16177791, FT ECO:0000269|PubMed:17562709" FT /id="VAR_060331" FT VARIANT 148 FT /note="M -> T (in allele B and allele D; dbSNP:rs17071550)" FT /evidence="ECO:0000269|PubMed:17562709" FT /id="VAR_012472" FT VARIANT 181 FT /note="I -> A (in allele D; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:17562709" FT /id="VAR_064572" FT VARIANT 181 FT /note="I -> T (in allele B and allele C)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17562709" FT /id="VAR_012473" FT VARIANT 188 FT /note="R -> W (in allele D; dbSNP:rs1506419)" FT /evidence="ECO:0000269|PubMed:17562709" FT /id="VAR_060332" FT VARIANT 293 FT /note="I -> T (in dbSNP:rs1395266)" FT /evidence="ECO:0000269|PubMed:17562709" FT /id="VAR_060333" FT VARIANT 303 FT /note="P -> S (in dbSNP:rs1395267)" FT /evidence="ECO:0000269|PubMed:17562709" FT /id="VAR_060334" FT VARIANT 354 FT /note="I -> T (in dbSNP:rs34811964)" FT /id="VAR_057177" FT CONFLICT 12 FT /note="C -> R (in Ref. 1; AAV73921)" FT /evidence="ECO:0000305" FT CONFLICT 43 FT /note="L -> P (in Ref. 1; AAV73923)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="F -> S (in Ref. 1; AAV73920)" FT /evidence="ECO:0000305" FT CONFLICT 267 FT /note="T -> A (in Ref. 1; AAV73920)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="V -> A (in Ref. 1; AAV73921)" FT /evidence="ECO:0000305" SQ SEQUENCE 392 AA; 44099 MW; 906F6DD412BCD756 CRC64; MGSLSTANVE FCLDVFKELN SNNIGDNIFF SSLSLLYALS MVLLGARGET AEQLEKVLHF SHTVDSLKPG FKDSPKCSQA GRIHSEFGVE FSQINQPDSN CTLSIANRLY GTKTMAFHQQ YLSCSEKWYQ ARLQTVDFEQ STEETRKMIN AWVENKTNGK VANLFGKSTI DPSSVMVLVN IIYFKGQRQN KFQVRETVKS PFQLSEGKNV TVEMMYQIGT FKLAFVKEPQ MQVLELPYVN NKLSMIILLP VGIANLKQIE KQLNSGTFHE WTSSSNMMER EVEVHLPRFK LEIKYELNSL LKPLGVTDLF NQVKADLSGM SPTKGLYLSK AIHKSYLDVS EEGTEAAAAT GDSIAVKSLP MRAQFKANHP FLFFIRHTHT NTILFCGKLA SP //