SPZ1_ARATH
ID SPZ1_ARATH Reviewed; 385 AA.
AC Q9SH52;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serpin-Z1;
DE AltName: Full=ArathZ1;
GN OrderedLocusNames=At1g64030; ORFNames=F22C12.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18060440; DOI=10.1007/s10142-007-0059-2;
RA Roberts T.H., Hejgaard J.;
RT "Serpins in plants and green algae.";
RL Funct. Integr. Genomics 8:1-27(2008).
CC -!- FUNCTION: Probable serine protease inhibitor. {ECO:0000250}.
CC -!- INDUCTION: By beta-amino-butyric acid (BABA) and infection by
CC Pseudomonas pathogen. {ECO:0000269|PubMed:18060440}.
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 carboxyl group of the serpin reactive site
CC and the serine hydroxyl of the protease. The resulting inactive serpin-
CC protease complex is highly stable (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007764; AAF24568.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34182.1; -; Genomic_DNA.
DR PIR; B96665; B96665.
DR RefSeq; NP_176586.1; NM_105076.2.
DR AlphaFoldDB; Q9SH52; -.
DR SMR; Q9SH52; -.
DR STRING; 3702.AT1G64030.1; -.
DR PaxDb; Q9SH52; -.
DR PRIDE; Q9SH52; -.
DR ProteomicsDB; 226913; -.
DR EnsemblPlants; AT1G64030.1; AT1G64030.1; AT1G64030.
DR GeneID; 842706; -.
DR Gramene; AT1G64030.1; AT1G64030.1; AT1G64030.
DR KEGG; ath:AT1G64030; -.
DR Araport; AT1G64030; -.
DR TAIR; locus:2024532; AT1G64030.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_4_0_1; -.
DR InParanoid; Q9SH52; -.
DR OMA; QFNRDQD; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9SH52; -.
DR PRO; PR:Q9SH52; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SH52; baseline and differential.
DR Genevisible; Q9SH52; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
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; 2.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 2: Evidence at transcript level;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT CHAIN 1..385
FT /note="Serpin-Z1"
FT /id="PRO_0000334546"
FT REGION 317..341
FT /note="RCL"
FT SITE 331..332
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
SQ SEQUENCE 385 AA; 42987 MW; 2DB5F425B9A86B90 CRC64;
MDVREAMKNQ THVAMILSGH VLSSAPKDSN VIFSPASINS AITMHAAGPG GDLVSGQILS
FLRSSSIDEL KTVFRELASV VYADRSATGG PKITAANGLW IDKSLPTDPK FKDLFENFFK
AVYVPVDFRS EAEEVRKEVN SWVEHHTNNL IKDLLPDGSV TSLTNKIYAN ALSFKGAWKR
PFEKYYTRDN DFYLVNGTSV SVPFMSSYEN QYVRAYDGFK VLRLPYQRGS DDTNRKFSMY
FYLPDKKDGL DDLLEKMAST PGFLDSHIPT YRDELEKFRI PKFKIEFGFS VTSVLDRLGL
RSMSMYHKAC VEIDEEGAEA AAATADGDCG CSLDFVEPPK KIDFVADHPF LFLIREEKTG
TVLFVGQIFD PSGPCSGSNS DSDDY
