SPA3B_MOUSE
ID SPA3B_MOUSE Reviewed; 420 AA.
AC Q8BYY9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine protease inhibitor A3B;
DE Short=Serpin A3B;
DE Flags: Precursor;
GN Name=Serpina3b;
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 [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).
RN [2]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12659817; DOI=10.1016/s0888-7543(02)00041-1;
RA Forsyth S., Horvath A., Coughlin P.;
RT "A review and comparison of the murine alpha1-antitrypsin and alpha1-
RT antichymotrypsin multigene clusters with the human clade A serpins.";
RL Genomics 81:336-345(2003).
RN [3]
RP REGION RCL.
RX PubMed=15638460; DOI=10.1007/s00239-004-2640-9;
RA Horvath A.J., Forsyth S.L., Coughlin P.B.;
RT "Expression patterns of murine antichymotrypsin-like genes reflect
RT evolutionary divergence at the Serpina3 locus.";
RL J. Mol. Evol. 59:488-497(2004).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC protein and directs binding to the target protease. The protease
CC cleaves the serpin at the reactive site within the RCL, establishing a
CC covalent linkage between the serpin reactive site and the protease. The
CC resulting inactive serpin-protease complex is highly stable (By
CC similarity). Variability within the reactive center loop (RCL)
CC sequences of Serpina3 paralogs may determine target protease
CC specificity. {ECO:0000250}.
CC -!- MISCELLANEOUS: The single human alpha1-antichymotrypsin gene (SERPINA3)
CC is represented by a cluster of 14 individual murine paralogs.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AK037160; BAC29726.1; -; mRNA.
DR CCDS; CCDS26147.1; -.
DR RefSeq; NP_766612.1; NM_173024.3.
DR AlphaFoldDB; Q8BYY9; -.
DR SMR; Q8BYY9; -.
DR STRING; 10090.ENSMUSP00000082127; -.
DR MEROPS; I04.056; -.
DR GlyGen; Q8BYY9; 2 sites.
DR iPTMnet; Q8BYY9; -.
DR PhosphoSitePlus; Q8BYY9; -.
DR MaxQB; Q8BYY9; -.
DR PaxDb; Q8BYY9; -.
DR PRIDE; Q8BYY9; -.
DR ProteomicsDB; 257295; -.
DR DNASU; 271047; -.
DR Ensembl; ENSMUST00000085052; ENSMUSP00000082127; ENSMUSG00000066364.
DR GeneID; 271047; -.
DR KEGG; mmu:271047; -.
DR UCSC; uc007owu.1; mouse.
DR CTD; 271047; -.
DR MGI; MGI:2182835; Serpina3b.
DR VEuPathDB; HostDB:ENSMUSG00000066364; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_2_1_1; -.
DR InParanoid; Q8BYY9; -.
DR OMA; ANGICFR; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q8BYY9; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 271047; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BYY9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BYY9; protein.
DR Bgee; ENSMUSG00000066364; Expressed in zone of skin and 13 other tissues.
DR ExpressionAtlas; Q8BYY9; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
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; 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.
PE 2: Evidence at transcript level;
KW Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..420
FT /note="Serine protease inhibitor A3B"
FT /id="PRO_0000032415"
FT REGION 367..392
FT /note="RCL"
FT SITE 381..382
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 47415 MW; 6758CD2048E971C2 CRC64;
MAFIAALGLL MAEICPAVIC CSDGTLGMHN AVQKGQDTQK QLDSLTLASI NTDFAFSFYK
ELALKNPHKN IAFSPFGIAT ALNSLTLGAK GNTLEEILEV LKFNLTETSE ADIHQGFKHL
LQRLSHPGDQ VQIRTGNALF VEKHLQILAE FKEKARALYH TEVFTANFQQ PHEAMKLINS
YMSNQTQGKI KELVSDMDGN TSMVIVNDLF FKAEWMVPFN SDDTFMGKFI VDRSRHVKVP
MMKTKNLRTP YFRDEELKCT VVELNYKGNG KAMFILPDQG KMQQVEASLQ PGTLKKWRKS
LRPRKIKELH LPKFSLSQHY NLEDILPELG IRELFSTQAD LSGITGVKNI TVSEMIHSTE
LDMTEKGTEG DAITIVGYNF MSAKLKPVFV KFEDQFLYIV LDQGDLWIHV MGKVINPSEK
