SPB11_HUMAN
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 03-AUG-2022, entry version 140.
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}.
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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 AlphaFoldDB; Q96P15; -.
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 Antibodypedia; 23130; 131 antibodies from 20 providers.
DR DNASU; 89778; -.
DR Ensembl; ENST00000382749.9; ENSP00000421854.1; ENSG00000206072.13.
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; Tissue enhanced (esophagus, prostate).
DR MIM; 615682; gene.
DR neXtProt; NX_Q96P15; -.
DR PharmGKB; PA37860; -.
DR VEuPathDB; HostDB:ENSG00000206072; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q96P15; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q96P15; -.
DR PathwayCommons; Q96P15; -.
DR BioGRID-ORCS; 89778; 3 hits in 198 CRISPR screens.
DR ChiTaRS; SERPINB11; human.
DR GenomeRNAi; 89778; -.
DR Pharos; Q96P15; Tbio.
DR PRO; PR:Q96P15; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96P15; protein.
DR Bgee; ENSG00000206072; Expressed in olfactory segment of nasal mucosa and 78 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
