SPZ4_HORVU
ID SPZ4_HORVU Reviewed; 399 AA.
AC P06293; Q40076;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serpin-Z4;
DE AltName: Full=BSZ4;
DE AltName: Full=HorvuZ4;
DE AltName: Full=Major endosperm albumin;
DE AltName: Full=Protein Z4;
DE Short=Protein Z;
GN Name=PAZ1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Carlsberg II; TISSUE=Grain;
RX PubMed=2269280; DOI=10.1111/j.1432-1033.1990.tb15644.x;
RA Brandt A., Svendsen I., Hejgaard J.;
RT "A plant serpin gene. Structure, organization and expression of the gene
RT encoding barley protein Z4.";
RL Eur. J. Biochem. 194:499-505(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Bomi; TISSUE=Endosperm;
RX PubMed=8810262; DOI=10.1074/jbc.271.41.25083;
RA Dahl S.W., Rasmussen S.K., Hejgaard J.;
RT "Heterologous expression of three plant serpins with distinct inhibitory
RT specificities.";
RL J. Biol. Chem. 271:25083-25088(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 220-399, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Carlsberg II; TISSUE=Grain;
RA Hejgaard J., Rasmussen S.K., Brandt A., Svendsen I.;
RT "Sequence homology between barley endosperm protein Z and protease
RT inhibitors of the alpha-1-antitrypsin family.";
RL FEBS Lett. 180:89-94(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 360-384.
RA Rasmussen S.K., Hopp H.E., Brandt A., Svendsen I., Hejgaard J.;
RT "A cDNA clone for protein Z, a major barley endosperm albumin.";
RL Carlsberg Res. Commun. 49:385-390(1984).
RN [5]
RP PROTEIN SEQUENCE OF 6-15 AND 362-367, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Alexis; TISSUE=Root;
RX PubMed=14504298; DOI=10.1093/jxb/erg248;
RA Roberts T.H., Marttila S., Rasmussen S.K., Hejgaard J.;
RT "Differential gene expression for suicide-substrate serine proteinase
RT inhibitors (serpins) in vegetative and grain tissues of barley.";
RL J. Exp. Bot. 54:2251-2263(2003).
CC -!- FUNCTION: A major component of the endosperm albumin, this protein acts
CC as a storage protein during grain filling, contributing a substantial
CC part of the grain's lysine. May have an inhibitory function during
CC filling or germination. Inhibits cathepsin G in vitro.
CC {ECO:0000269|PubMed:8810262}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryo and endosperm. Is
CC accumulated and stored in the endosperm, where it exists in a free and
CC a bound form. Expressed in roots, coleoptiles, shoots and leaves.
CC {ECO:0000269|PubMed:14504298}.
CC -!- DEVELOPMENTAL STAGE: Synthesized 10-25 days after fertilization
CC (developing endosperm).
CC -!- INDUCTION: Its expression is regulated by the 'high lysine' alleles
CC Lys1 and Lys3a.
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; X51726; CAA36015.1; -; Genomic_DNA.
DR EMBL; X97636; CAA66232.1; -; mRNA.
DR EMBL; X05902; CAA29331.1; -; mRNA.
DR EMBL; M35065; AAA32971.1; -; mRNA.
DR PIR; S13822; DXBHZ.
DR AlphaFoldDB; P06293; -.
DR SMR; P06293; -.
DR IntAct; P06293; 1.
DR Allergome; 951; Hor v 33.
DR MEROPS; I04.065; -.
DR PRIDE; P06293; -.
DR ExpressionAtlas; P06293; baseline.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; 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 1: Evidence at protein level;
KW Direct protein sequencing; Plant defense; Protease inhibitor;
KW Seed storage protein; Serine protease inhibitor; Storage protein.
FT CHAIN 1..399
FT /note="Serpin-Z4"
FT /id="PRO_0000094133"
FT REGION 36..56
FT /note="Signal for targeting protein Z4 into the ER lumen"
FT /evidence="ECO:0000255"
FT REGION 343..367
FT /note="RCL"
FT SITE 357..358
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
FT CONFLICT 24
FT /note="R -> A (in Ref. 2; CAA66232)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> GG (in Ref. 2; CAA66232)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> V (in Ref. 2; CAA66232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 43276 MW; 023B8E52475ABA56 CRC64;
MATTLATDVR LSIAHQTRFA LRLRSAISSN PERAAGNVAF SPLSLHVALS LITAGAAATR
DQLVAILGDG GAGDAKELNA LAEQVVQFVL ANESSTGGPR IAFANGIFVD ASLSLKPSFE
ELAVCQYKAK TQSVDFQHKT LEAVGQVNSW VEQVTTGLIK QILPPGSVDN TTKLILGNAL
YFKGAWDQKF DESNTKCDSF HLLDGSSIQT QFMSSTKKQY ISSSDNLKVL KLPYAKGHDK
RQFSMYILLP GAQDGLWSLA KRLSTEPEFI ENHIPKQTVE VGRFQLPKFK ISYQFEASSL
LRALGLQLPF SEEADLSEMV DSSQGLEISH VFHKSFVEVN EEGTEAGAAT VAMGVAMSMP
LKVDLVDFVA NHPFLFLIRE DIAGVVVFVG HVTNPLISA
