SPB12_MOUSE
ID SPB12_MOUSE Reviewed; 423 AA.
AC Q9D7P9; Q6UKZ3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serpin B12;
GN Name=Serpinb12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=15203215; DOI=10.1016/j.ygeno.2004.01.015;
RA Askew D.J., Askew Y.S., Kato Y., Turner R.F., Dewar K., Lehoczky J.,
RA Silverman G.A.;
RT "Comparative genomic analysis of the clade B serpin cluster at human
RT chromosome 18q21: amplification within the mouse squamous cell carcinoma
RT antigen gene locus.";
RL Genomics 84:176-184(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw, and Limb;
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: Inhibits trypsin and plasmin, but not thrombin, coagulation
CC factor Xa, or urokinase-type plasminogen activator. May play a role in
CC cell differentiation. {ECO:0000250|UniProtKB:Q96P63}.
CC -!- SUBUNIT: Interacts with SLFN12; as part of a pathway regulating cell
CC differentiation. {ECO:0000250|UniProtKB:Q96P63}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; AY367773; AAR89287.1; -; mRNA.
DR EMBL; AK009018; BAB26028.1; -; mRNA.
DR EMBL; AK040697; BAC30672.1; -; mRNA.
DR EMBL; BC062134; AAH62134.1; -; mRNA.
DR CCDS; CCDS15212.1; -.
DR RefSeq; NP_001186142.1; NM_001199213.1.
DR RefSeq; NP_082247.1; NM_027971.2.
DR AlphaFoldDB; Q9D7P9; -.
DR SMR; Q9D7P9; -.
DR STRING; 10090.ENSMUSP00000080030; -.
DR MEROPS; I04.016; -.
DR iPTMnet; Q9D7P9; -.
DR PhosphoSitePlus; Q9D7P9; -.
DR MaxQB; Q9D7P9; -.
DR PaxDb; Q9D7P9; -.
DR PRIDE; Q9D7P9; -.
DR ProteomicsDB; 261493; -.
DR Antibodypedia; 10036; 212 antibodies from 23 providers.
DR DNASU; 71869; -.
DR Ensembl; ENSMUST00000081277; ENSMUSP00000080030; ENSMUSG00000059956.
DR Ensembl; ENSMUST00000112724; ENSMUSP00000108344; ENSMUSG00000059956.
DR GeneID; 71869; -.
DR KEGG; mmu:71869; -.
DR UCSC; uc007chc.2; mouse.
DR CTD; 89777; -.
DR MGI; MGI:1919119; Serpinb12.
DR VEuPathDB; HostDB:ENSMUSG00000059956; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161829; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; Q9D7P9; -.
DR OMA; CYFGKLL; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9D7P9; -.
DR TreeFam; TF352619; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 71869; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9D7P9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D7P9; protein.
DR Bgee; ENSMUSG00000059956; Expressed in esophagus and 43 other tissues.
DR Genevisible; Q9D7P9; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
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 Cytoplasm; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..423
FT /note="Serpin B12"
FT /id="PRO_0000094120"
FT REGION 63..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 388..389
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CONFLICT 67
FT /note="E -> G (in Ref. 1; AAR89287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47835 MW; 5A22BE2FE51B6120 CRC64;
MDSLTAANNK FCFDFFREIS KDDAHKNIFV CPLSLSAAFG MVRLGARGDS AHQIDEALHF
NELSKDEHKE PNDPSPQSES KASDSSLEGQ KQTSASQDQQ GESTNDHQLL GCHFGKLLSR
IDRDKSYYTL SMANRLYGEQ EFPICSEYSD DVTEFFHTTV ESVDFQKDSE KSRQEINFWV
ESQSQGKIKE LFGKEAIDNS TVLVLVNAVY FKAKWEREFN SENTVDASFC LNENEKKTVK
MMNQKGKFRI GFIDELQAQI LEMKYAMGKL SMLVLLPSCS EDNVNSLQEL EKKINHEKLL
AWSSSENLSE KPVAISFPQF NLEDSYDLKS ILQDMGIKDV FDETKADLTG ISKSPNLYLS
KIVHKTFVEV DEMGTQAAAA SGVVAAEKAL PSWVEFNANH PFLFFIRHNP TQSLLFCGRV
YCP
