SPA3K_MOUSE
ID SPA3K_MOUSE Reviewed; 418 AA.
AC P07759; Q62257; Q8VCH3; Q91W80; Q91X80;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Serine protease inhibitor A3K;
DE Short=Serpin A3K;
DE AltName: Full=Contrapsin;
DE AltName: Full=SPI-2;
DE Flags: Precursor;
GN Name=Serpina3k; Synonyms=Mcm2, Spi2;
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=2277027; DOI=10.1093/oxfordjournals.jbchem.a123204;
RA Suzuki Y., Yamamoto K., Sinohara H.;
RT "Molecular cloning and sequence analysis of full-length cDNA coding for
RT mouse contrapsin.";
RL J. Biochem. 108:344-346(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-41; 67-83; 156-176;
RP 218-227; 229-235 AND 315-334, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2049065; DOI=10.1042/bj2760337;
RA Ohkubo K., Ogata S., Misumi Y., Takami N., Sinohara H., Ikehara Y.;
RT "Cloning, structure and expression of cDNA for mouse contrapsin and a
RT related protein.";
RL Biochem. J. 276:337-342(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11916263; DOI=10.3109/10425170109025005;
RA Yoshida K., Suzuki Y., Sinohara H.;
RT "Molecular cloning and sequence analysis of C57BL/6 mouse contrapsin
RT cDNA.";
RL DNA Seq. 12:289-291(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-418.
RX PubMed=6547997; DOI=10.1038/311175a0;
RA Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.;
RT "Plasma protease inhibitors in mouse and man: divergence within the
RT reactive centre regions.";
RL Nature 311:175-177(1984).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=6214866; DOI=10.1016/0049-3848(82)90276-6;
RA Takahara H., Sinohara H.;
RT "Mouse plasma trypsin inhibitors: inhibitory spectrum of contrapsin and
RT alpha-1-antitrypsin.";
RL Thromb. Res. 27:45-50(1982).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=6224776; DOI=10.1093/oxfordjournals.jbchem.a134276;
RA Takahara H., Sinohara H.;
RT "Inhibitory spectrum of mouse contrapsin and alpha-1-antitrypsin against
RT mouse serine proteases.";
RL J. Biochem. 93:1411-1419(1983).
RN [9]
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 [10]
RP TISSUE SPECIFICITY, AND 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).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-270.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-270.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Contrapsin inhibits trypsin-like proteases.
CC {ECO:0000269|PubMed:6214866, ECO:0000269|PubMed:6224776}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in liver and secreted in plasma.
CC {ECO:0000269|PubMed:15638460, ECO:0000269|PubMed:2049065,
CC ECO:0000269|PubMed:6214866, ECO:0000269|PubMed:6224776}.
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; D00725; BAA00627.1; -; mRNA.
DR EMBL; X55147; CAA38948.1; -; mRNA.
DR EMBL; X56786; CAA40106.1; -; mRNA.
DR EMBL; AK149436; BAE28874.1; -; mRNA.
DR EMBL; BC011217; AAH11217.1; -; mRNA.
DR EMBL; BC016407; AAH16407.1; -; mRNA.
DR EMBL; BC019802; AAH19802.1; -; mRNA.
DR EMBL; X00946; CAA25458.1; -; Genomic_DNA.
DR CCDS; CCDS36537.1; -.
DR PIR; JX0129; JX0129.
DR RefSeq; NP_035588.2; NM_011458.2.
DR AlphaFoldDB; P07759; -.
DR SMR; P07759; -.
DR BioGRID; 203440; 7.
DR IntAct; P07759; 2.
DR STRING; 10090.ENSMUSP00000042095; -.
DR MEROPS; I04.029; -.
DR GlyConnect; 781; 3 N-Linked glycans (2 sites).
DR GlyGen; P07759; 4 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; P07759; -.
DR PhosphoSitePlus; P07759; -.
DR CPTAC; non-CPTAC-4063; -.
DR jPOST; P07759; -.
DR MaxQB; P07759; -.
DR PaxDb; P07759; -.
DR PeptideAtlas; P07759; -.
DR PRIDE; P07759; -.
DR ProteomicsDB; 263306; -.
DR DNASU; 20714; -.
DR GeneID; 20714; -.
DR KEGG; mmu:20714; -.
DR UCSC; uc007oxd.1; mouse.
DR CTD; 20714; -.
DR MGI; MGI:98377; Serpina3k.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P07759; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P07759; -.
DR TreeFam; TF343201; -.
DR BioGRID-ORCS; 20714; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Serpina3k; mouse.
DR PRO; PR:P07759; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P07759; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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 GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2049065"
FT CHAIN 22..418
FT /note="Serine protease inhibitor A3K"
FT /id="PRO_0000032417"
FT REGION 369..394
FT /note="RCL"
FT SITE 384..385
FT /note="Reactive bond"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CONFLICT 15
FT /note="I -> V (in Ref. 5; AAH19802/AAH11217/AAH16407)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..70
FT /note="PDT -> QDK (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> F (in Ref. 5; AAH16407)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> R (in Ref. 2; CAA38948)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="E -> K (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="ER -> DG (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="M -> V (in Ref. 6; CAA25458)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="T -> A (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="P -> S (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="N -> D (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="T -> I (in Ref. 6; CAA25458)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> A (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="I -> V (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="A -> G (in Ref. 5; AAH19802)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="H -> C (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="F -> I (in Ref. 3; CAA40106 and 4; BAE28874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46880 MW; 761A6F986C5B5CCD CRC64;
MAFIVAMGMI LMAGICPAVL CFPDGTKEMD IVFHEHQDNG TQDDSLTLAS VNTDFAFSLY
KKLALKNPDT NIVFSPLSIS AALALVSLGA KGKTMEEILE GLKFNLTETP EADIHQGFGN
LLQSLSQPED QDQINIGNAM FIEKDLQILA EFHEKTRALY QTEAFTADFQ QPTEAKNLIN
DYVSNQTQGM IKELISELDE RTLMVLVNYI YFKGKWKISF DPQDTFESEF YLDEKRSVKV
PMMKMKLLTT RHFRDEELSC SVLELKYTGN ASALLILPDQ GRMQQVEASL QPETLRKWRK
TLFPSQIEEL NLPKFSIASN YRLEEDVLPE MGIKEVFTEQ ADLSGITETK KLSVSQVVHK
AVLDVAETGT EAAAATGVIG GIRKAILPAV HFNRPFLFVI YHTSAQSILF MAKVNNPK
