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Aspartyl protease APCB1 (EC 3.4.23.-) (Aspartyl protease cleaving BAG 1)

 APCB1_ARATH             Reviewed;         583 AA.
Q9M9A8; A8MQI7;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 130.
RecName: Full=Aspartyl protease APCB1 {ECO:0000303|PubMed:26739014};
EC=3.4.23.- {ECO:0000305};
AltName: Full=Aspartyl protease cleaving BAG 1 {ECO:0000303|PubMed:26739014};
Name=APCB1 {ECO:0000303|PubMed:26739014};
OrderedLocusNames=At1g49050 {ECO:0000312|Araport:AT1G49050};
ORFNames=F27J15.15 {ECO:0000312|EMBL:AAF69716.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY.
PubMed=16381599; DOI=10.2174/138920305774933268;
Faro C., Gal S.;
"Aspartic proteinase content of the Arabidopsis genome.";
Curr. Protein Pept. Sci. 6:493-500(2005).
[5]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BAG6 AND BAGP1, AND
MUTAGENESIS OF ASP-223 AND ASP-431.
PubMed=26739014; DOI=10.1105/tpc.15.00626;
Li Y., Kabbage M., Liu W., Dickman M.B.;
"Aspartyl protease-mediated cleavage of BAG6 is necessary for
autophagy and fungal resistance in plants.";
Plant Cell 28:233-247(2016).
-!- FUNCTION: Involved in proteolytic processing of BAG6 and plant
basal immunity. {ECO:0000269|PubMed:26739014}.
-!- SUBUNIT: Interacts with BAG6 and BAGP1.
{ECO:0000269|PubMed:26739014}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9M9A8-1; Sequence=Displayed;
Name=2;
IsoId=Q9M9A8-2; Sequence=VSP_058207;
-!- DISRUPTION PHENOTYPE: Enhanced susceptibility to B.cinerea and
permissive fungal growth. {ECO:0000269|PubMed:26739014}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AC016041; AAF69716.1; -; Genomic_DNA.
EMBL; CP002684; AEE32388.1; -; Genomic_DNA.
EMBL; CP002684; AEE32389.1; -; Genomic_DNA.
EMBL; AF360182; AAK25892.1; -; mRNA.
EMBL; AY039998; AAK64075.1; -; mRNA.
RefSeq; NP_001077691.1; NM_001084222.1. [Q9M9A8-2]
RefSeq; NP_564539.1; NM_103798.5. [Q9M9A8-1]
UniGene; At.20904; -.
ProteinModelPortal; Q9M9A8; -.
STRING; 3702.AT1G49050.1; -.
MEROPS; A01.A25; -.
PaxDb; Q9M9A8; -.
EnsemblPlants; AT1G49050.1; AT1G49050.1; AT1G49050. [Q9M9A8-1]
EnsemblPlants; AT1G49050.2; AT1G49050.2; AT1G49050. [Q9M9A8-2]
GeneID; 841328; -.
Gramene; AT1G49050.1; AT1G49050.1; AT1G49050. [Q9M9A8-1]
Gramene; AT1G49050.2; AT1G49050.2; AT1G49050. [Q9M9A8-2]
KEGG; ath:AT1G49050; -.
Araport; AT1G49050; -.
TAIR; locus:2028466; AT1G49050.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
HOGENOM; HOG000241781; -.
OMA; ARDDMHL; -.
OrthoDB; EOG093605TD; -.
PhylomeDB; Q9M9A8; -.
PRO; PR:Q9M9A8; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9M9A8; baseline and differential.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
CDD; cd05475; nucellin_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033823; Nucellin.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR032799; TAXi_C.
InterPro; IPR032861; TAXi_N.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF14541; TAXi_C; 1.
Pfam; PF14543; TAXi_N; 1.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 2.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Alternative splicing; Aspartyl protease; Complete proteome; Hydrolase;
Membrane; Protease; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 583 Aspartyl protease APCB1.
/FTId=PRO_0000436003.
TRANSMEM 83 103 Helical. {ECO:0000255}.
DOMAIN 203 564 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
COMPBIAS 8 12 Poly-Gln. {ECO:0000255}.
COMPBIAS 119 122 Poly-Asp. {ECO:0000255}.
ACT_SITE 223 223 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 431 431 {ECO:0000255|PROSITE-ProRule:PRU10094}.
VAR_SEQ 1 201 MEPDLHDQQQQQRVHSVVIITLPPSDDPSQGKTISAFTLTD
HDYPLEIPPEDNPNPSFQPDPLHRNQQSRLLFSDLSMNSPR
LVLGLLGISLLAVAFYASVFPNSVQMFRVSPDERNRDDDDN
LRETASFVFPVYHKLRAREFHERILEEDLGLENENFVESMD
LELVNPVKVNDVLSTSAGSIDSSTTIFPVGGNVYPDG ->
MFYLQVPVLLTPPLRFFPSVVMCIQMGM (in isoform
2).
/FTId=VSP_058207.
MUTAGEN 223 223 D->A: Loss of protease activity; when
associated with A-431.
{ECO:0000269|PubMed:26739014}.
MUTAGEN 431 431 D->A: Loss of protease activity; when
associated with A-223.
{ECO:0000269|PubMed:26739014}.
SEQUENCE 583 AA; 65349 MW; BBF94DFA162E5122 CRC64;
MEPDLHDQQQ QQRVHSVVII TLPPSDDPSQ GKTISAFTLT DHDYPLEIPP EDNPNPSFQP
DPLHRNQQSR LLFSDLSMNS PRLVLGLLGI SLLAVAFYAS VFPNSVQMFR VSPDERNRDD
DDNLRETASF VFPVYHKLRA REFHERILEE DLGLENENFV ESMDLELVNP VKVNDVLSTS
AGSIDSSTTI FPVGGNVYPD GLYYTRILVG KPEDGQYYHL DIDTGSELTW IQCDAPCTSC
AKGANQLYKP RKDNLVRSSE AFCVEVQRNQ LTEHCENCHQ CDYEIEYADH SYSMGVLTKD
KFHLKLHNGS LAESDIVFGC GYDQQGLLLN TLLKTDGILG LSRAKISLPS QLASRGIISN
VVGHCLASDL NGEGYIFMGS DLVPSHGMTW VPMLHDSRLD AYQMQVTKMS YGQGMLSLDG
ENGRVGKVLF DTGSSYTYFP NQAYSQLVTS LQEVSGLELT RDDSDETLPI CWRAKTNFPF
SSLSDVKKFF RPITLQIGSK WLIISRKLLI QPEDYLIISN KGNVCLGILD GSSVHDGSTI
ILGDISMRGH LIVYDNVKRR IGWMKSDCVR PREIDHNVPF FQG


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