SPB7_MOUSE
ID SPB7_MOUSE Reviewed; 380 AA.
AC Q9D695;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serpin B7;
DE AltName: Full=Megsin;
GN Name=Serpinb7;
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].
RX PubMed=11473647; DOI=10.1046/j.1523-1755.2001.060002641.x;
RA Nangaku M., Miyata T., Suzuki D., Umezono T., Hashimoto T., Wada T.,
RA Yagi M., Nagano N., Inagi R., Kurokawa K.;
RT "Cloning of rodent megsin revealed its up-regulation in
RT mesangioproliferative nephritis.";
RL Kidney Int. 60:641-652(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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).
CC -!- FUNCTION: Might function as an inhibitor of Lys-specific proteases.
CC Might influence the maturation of megakaryocytes via its action as a
CC serpin (By similarity). {ECO:0000250}.
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; AF105328; AAL16768.1; -; mRNA.
DR EMBL; AK014524; BAB29410.1; -; mRNA.
DR CCDS; CCDS35686.1; -.
DR RefSeq; NP_081824.1; NM_027548.3.
DR AlphaFoldDB; Q9D695; -.
DR SMR; Q9D695; -.
DR BioGRID; 228047; 1.
DR STRING; 10090.ENSMUSP00000083896; -.
DR MEROPS; I04.012; -.
DR iPTMnet; Q9D695; -.
DR PhosphoSitePlus; Q9D695; -.
DR MaxQB; Q9D695; -.
DR PaxDb; Q9D695; -.
DR PRIDE; Q9D695; -.
DR ProteomicsDB; 257341; -.
DR Antibodypedia; 10160; 186 antibodies from 26 providers.
DR DNASU; 116872; -.
DR Ensembl; ENSMUST00000086690; ENSMUSP00000083896; ENSMUSG00000067001.
DR GeneID; 116872; -.
DR KEGG; mmu:116872; -.
DR UCSC; uc007chm.2; mouse.
DR CTD; 8710; -.
DR MGI; MGI:2151053; Serpinb7.
DR VEuPathDB; HostDB:ENSMUSG00000067001; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000161520; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; Q9D695; -.
DR OMA; FREMDNN; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9D695; -.
DR TreeFam; TF352619; -.
DR BioGRID-ORCS; 116872; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9D695; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D695; protein.
DR Bgee; ENSMUSG00000067001; Expressed in skin of external ear and 25 other tissues.
DR ExpressionAtlas; Q9D695; baseline and differential.
DR Genevisible; Q9D695; MM.
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 GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISO:MGI.
DR GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISO:MGI.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; ISO:MGI.
DR GO; GO:0030162; P:regulation of proteolysis; ISO:MGI.
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; Phosphoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..380
FT /note="Serpin B7"
FT /id="PRO_0000094109"
FT SITE 347..348
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75635"
SQ SEQUENCE 380 AA; 43050 MW; C9240272BCFB9CF4 CRC64;
MASLAAANAE FGFDLFREMD SSQGNGNVFF SSLSIFTALT LIRLGARGDC ARQIDKALHF
NIPSRQGNSS NNQPGLQYQL KRVLADINSS HKDYELSIAT GVFAEKVYDF HKNYIECAEN
LYNAKVERVD FTNDVQDTRF KINKWIENET HGKIKKVLGD SSLSSSAVMV LVNAVYFKGK
WKSAFTKTDT LSCRFRSPTC PGKVVNMMHQ ERRFNLSTIQ QPPMQVLELQ YHGGISMYIM
LPEDGLCEIE SKLSFQNLMD WTNRRKMKSQ YVNVFLPQFK IEKNYEMTHH LKSLGLKDIF
DESSADLSGI ASGGRLYVSK LMHKSFIEVS EEGTEATAAT ENNIVEKQLP ESTVFRADRP
FLFVIKKNDI ILFTGKVSCP
