SPA3L_RAT
ID SPA3L_RAT Reviewed; 413 AA.
AC P05544;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine protease inhibitor A3L;
DE Short=Serpin A3L;
DE AltName: Full=CPI-23;
DE AltName: Full=Contrapsin-like protease inhibitor 3;
DE AltName: Full=Serine protease inhibitor 1;
DE Short=SPI-1;
DE Flags: Precursor;
GN Name=Serpina3l; Synonyms=Spin2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1864837;
RA Ohkubo K., Ogata S., Misumi Y., Takami N., Ikehara Y.;
RT "Molecular cloning and characterization of rat contrapsin-like protease
RT inhibitor and related proteins.";
RL J. Biochem. 109:243-250(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-413, INDUCTION, AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=1694763; DOI=10.1111/j.1432-1033.1990.tb15587.x;
RA Pages G., Rouayrenc J.F., le Cam G., Mariller M., le Cam A.;
RT "Molecular characterization of three rat liver serine-protease inhibitors
RT affected by inflammation and hypophysectomy. Protein and mRNA analysis and
RT cDNA cloning.";
RL Eur. J. Biochem. 190:385-391(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-403, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=3494016; DOI=10.1016/s0021-9258(18)61345-6;
RA Yoon J.-B., Towle H.C., Seelig S.;
RT "Growth hormone induces two mRNA species of the serine protease inhibitor
RT gene family in rat liver.";
RL J. Biol. Chem. 262:4284-4289(1987).
RN [5]
RP PROTEIN SEQUENCE OF 142-152; 188-210 AND 233-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1864837}.
CC -!- INDUCTION: By growth hormone. Reduced during acute inflammation.
CC {ECO:0000269|PubMed:1694763, ECO:0000269|PubMed:3494016}.
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1694763}.
CC -!- MISCELLANEOUS: The single human alpha1-antichymotrypsin gene (SERPINA3)
CC is represented by a cluster of 6 individual rat paralogs.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
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DR EMBL; D00752; BAA00649.1; -; mRNA.
DR EMBL; BC088096; AAH88096.1; -; mRNA.
DR EMBL; X16357; CAA34406.1; -; mRNA.
DR EMBL; M15917; AAA42172.1; -; mRNA.
DR PIR; S08102; S08102.
DR AlphaFoldDB; P05544; -.
DR SMR; P05544; -.
DR MEROPS; I04.050; -.
DR GlyGen; P05544; 4 sites.
DR iPTMnet; P05544; -.
DR PRIDE; P05544; -.
DR Ensembl; ENSRNOT00000087017; ENSRNOP00000070308; ENSRNOG00000010478.
DR UCSC; RGD:3745; rat.
DR RGD; 3745; LOC299282.
DR GeneTree; ENSGT00940000154392; -.
DR InParanoid; P05544; -.
DR PRO; PR:P05544; -.
DR Proteomes; UP000002494; Chromosome 6.
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 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; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..413
FT /note="Serine protease inhibitor A3L"
FT /id="PRO_0000032422"
FT REGION 365..389
FT /note="RCL"
FT SITE 379..380
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 245
FT /note="V -> L (in Ref. 4; AAA42172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46277 MW; 3AACFAFA6AAA9BE7 CRC64;
MAFIAALGLL MAGICPAVLC DGTLGRDTLS HEDHGKGRQL HSLTLASSNT DFALSLYKKL
ALRNPDKNVV FSPLSISAAL TILSLGAKDS TMEEILEGLK FNLTEITEEE IHQGFGHLLQ
RLSQPEDQVE INTGSALFID KEQPILSEFQ EKTRALYQAE AFIADFKQPN EAKKLINDYV
SNQTQGKIAE LFSDLEERTS MVLVNYLLFK GKWKVPFNPN DTFESEFYLD EKRSVKVPMM
KIKEVTTPYV RDEELSCSVL ELKYTGNASA LFILPDQGKM QQVESSLQPE TLKKWKDSLI
PRIINDLRMP KFSISTDYSL KEVLPELGIK KVFSQQADLS RITGTKDLYV SQVVHKAVLD
VDETGTEATA ATGVATVIRR QPRTLNFNRP FMVVITDMDS QSILFVAKIT NPK
