SPZ4_ARATH
ID SPZ4_ARATH Reviewed; 393 AA.
AC Q9M1T7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serpin-Z4;
DE AltName: Full=ArathZ4;
GN OrderedLocusNames=At3g45220; ORFNames=T14D3.160;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 -!- 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}.
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DR EMBL; AL138649; CAB72160.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78005.1; -; Genomic_DNA.
DR PIR; T47462; T47462.
DR RefSeq; NP_190108.1; NM_114391.1.
DR AlphaFoldDB; Q9M1T7; -.
DR SMR; Q9M1T7; -.
DR STRING; 3702.AT3G45220.1; -.
DR PaxDb; Q9M1T7; -.
DR PRIDE; Q9M1T7; -.
DR ProteomicsDB; 226914; -.
DR EnsemblPlants; AT3G45220.1; AT3G45220.1; AT3G45220.
DR GeneID; 823658; -.
DR Gramene; AT3G45220.1; AT3G45220.1; AT3G45220.
DR KEGG; ath:AT3G45220; -.
DR Araport; AT3G45220; -.
DR TAIR; locus:2096910; AT3G45220.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_023330_4_0_1; -.
DR InParanoid; Q9M1T7; -.
DR OMA; CYFGKLL; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q9M1T7; -.
DR PRO; PR:Q9M1T7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1T7; baseline and differential.
DR Genevisible; Q9M1T7; AT.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT CHAIN 1..393
FT /note="Serpin-Z4"
FT /id="PRO_0000334549"
FT REGION 342..366
FT /note="RCL"
FT SITE 356..357
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 44170 MW; 6484CB33A990D204 CRC64;
MELGKSMENQ TDVMVLLAKH VIPTVANGSN LVFSPMSINV LLCLIAAGSN CVTKEQILSF
IMLPSSDYLN AVLAKTVSVA LNDGMERSDL HLSTAYGVWI DKSLSFKPSF KDLLENSYNA
TCNQVDFATK PAEVINEVNA WAEVHTNGLI KEILSDDSIK TIRESMLILA NAVYFKGAWS
KKFDAKLTKS YDFHLLDGTM VKVPFMTNYK KQYLEYYDGF KVLRLPYVED QRQFAMYIYL
PNDRDGLPTL LEEISSKPRF LDNHIPRQRI LTEAFKIPKF KFSFEFKASD VLKEMGLTLP
FTHGSLTEMV ESPSIPENLC VAENLFVSNV FHKACIEVDE EGTEAAAVSV ASMTKDMLLM
GDFVADHPFL FTVREEKSGV ILFMGQVLDP SIH
