SPA3A_MOUSE
ID SPA3A_MOUSE Reviewed; 422 AA.
AC Q6P4P1; Q9D490;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine protease inhibitor A3A;
DE Short=Serpin A3A;
DE Flags: Precursor;
GN Name=Serpina3a;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [3]
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 [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P4P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P4P1-2; Sequence=VSP_014229, VSP_014230;
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 alpha-1-antichymotrypsin gene
CC (SERPINA3) is represented by a cluster of 14 individual murine
CC paralogs.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AK016702; BAB30388.1; -; mRNA.
DR EMBL; BC063325; AAH63325.1; -; mRNA.
DR CCDS; CCDS49156.1; -. [Q6P4P1-1]
DR CCDS; CCDS79153.1; -. [Q6P4P1-2]
DR RefSeq; NP_083016.1; NM_028740.2. [Q6P4P1-2]
DR AlphaFoldDB; Q6P4P1; -.
DR SMR; Q6P4P1; -.
DR STRING; 10090.ENSMUSP00000140024; -.
DR MEROPS; I04.069; -.
DR GlyGen; Q6P4P1; 3 sites.
DR iPTMnet; Q6P4P1; -.
DR PhosphoSitePlus; Q6P4P1; -.
DR CPTAC; non-CPTAC-3500; -.
DR MaxQB; Q6P4P1; -.
DR PaxDb; Q6P4P1; -.
DR PeptideAtlas; Q6P4P1; -.
DR PRIDE; Q6P4P1; -.
DR ProteomicsDB; 263304; -. [Q6P4P1-1]
DR ProteomicsDB; 263305; -. [Q6P4P1-2]
DR DNASU; 74069; -.
DR Ensembl; ENSMUST00000109965; ENSMUSP00000105591; ENSMUSG00000041536. [Q6P4P1-2]
DR GeneID; 74069; -.
DR KEGG; mmu:74069; -.
DR UCSC; uc011yre.1; mouse. [Q6P4P1-2]
DR CTD; 74069; -.
DR MGI; MGI:1921319; Serpina3a.
DR VEuPathDB; HostDB:ENSMUSG00000041536; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154392; -.
DR HOGENOM; CLU_023330_6_0_1; -.
DR InParanoid; Q6P4P1; -.
DR OrthoDB; 1124079at2759; -.
DR BioGRID-ORCS; 74069; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q6P4P1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6P4P1; protein.
DR Bgee; ENSMUSG00000041536; Expressed in spermatocyte and 16 other tissues.
DR ExpressionAtlas; Q6P4P1; baseline and differential.
DR Genevisible; Q6P4P1; MM.
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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..422
FT /note="Serine protease inhibitor A3A"
FT /id="PRO_0000032414"
FT REGION 369..394
FT /note="RCL"
FT SITE 383..384
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014229"
FT VAR_SEQ 191..214
FT /note="KIKELVSDLHRNTSMALVNFLNFQ -> MRTVWLFQMFPFLLGPNIRQELLE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014230"
FT CONFLICT 264
FT /note="M -> V (in Ref. 2; AAH63325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47772 MW; 4656CF19C4D614BC CRC64;
MAFIAALGLL MVGICPAVTY WATADGQLGG HTAVQKDRDH EIQLDSVTLA SINTDFAFSL
YKKLALENPH KNIVFSPLSI SAALALMSLG AKGNTLEEIL EGLKFNLPET PEADIHQNFG
HLLQMLIQPE NQVQINAGNA LFIDKHLQIL TEFKEKARAL YKAEAFTTDF QRPREATKLI
NDYVRKQTQG KIKELVSDLH RNTSMALVNF LNFQGFWNVT FDPEDTFLGN FTLDRKRTVN
VPMMKTEELT TNYFRDEEMQ STVMELNYIG NASFLFILPD QGRIQHVEDS LQPQSLRKWR
KSLRPRMLDE LSLPKFSLSQ DYNLNDILPE LGIKEVFSTQ ADLSGITGAK NIRVSQMIHQ
AALDVTETHT EADVITIARY NFQSAKIKAK IVKVDREFLY LILDPMFKSI SVMGKVINPL
TN
