APCB1_ARATH
ID APCB1_ARATH Reviewed; 583 AA.
AC Q9M9A8; A8MQI7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aspartyl protease APCB1 {ECO:0000303|PubMed:26739014};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Aspartyl protease cleaving BAG 1 {ECO:0000303|PubMed:26739014};
GN Name=APCB1 {ECO:0000303|PubMed:26739014};
GN OrderedLocusNames=At1g49050 {ECO:0000312|Araport:AT1G49050};
GN ORFNames=F27J15.15 {ECO:0000312|EMBL:AAF69716.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=16381599; DOI=10.2174/138920305774933268;
RA Faro C., Gal S.;
RT "Aspartic proteinase content of the Arabidopsis genome.";
RL Curr. Protein Pept. Sci. 6:493-500(2005).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BAG6 AND BAGP1, AND
RP MUTAGENESIS OF ASP-223 AND ASP-431.
RX PubMed=26739014; DOI=10.1105/tpc.15.00626;
RA Li Y., Kabbage M., Liu W., Dickman M.B.;
RT "Aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and
RT fungal resistance in plants.";
RL Plant Cell 28:233-247(2016).
CC -!- FUNCTION: Involved in proteolytic processing of BAG6 and plant basal
CC immunity. {ECO:0000269|PubMed:26739014}.
CC -!- SUBUNIT: Interacts with BAG6 and BAGP1. {ECO:0000269|PubMed:26739014}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M9A8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M9A8-2; Sequence=VSP_058207;
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to B.cinerea and
CC permissive fungal growth. {ECO:0000269|PubMed:26739014}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AC016041; AAF69716.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32388.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32389.1; -; Genomic_DNA.
DR EMBL; AF360182; AAK25892.1; -; mRNA.
DR EMBL; AY039998; AAK64075.1; -; mRNA.
DR RefSeq; NP_001077691.1; NM_001084222.1. [Q9M9A8-2]
DR RefSeq; NP_564539.1; NM_103798.5. [Q9M9A8-1]
DR AlphaFoldDB; Q9M9A8; -.
DR SMR; Q9M9A8; -.
DR STRING; 3702.AT1G49050.1; -.
DR MEROPS; A01.A25; -.
DR PaxDb; Q9M9A8; -.
DR PRIDE; Q9M9A8; -.
DR ProteomicsDB; 224556; -. [Q9M9A8-1]
DR EnsemblPlants; AT1G49050.1; AT1G49050.1; AT1G49050. [Q9M9A8-1]
DR EnsemblPlants; AT1G49050.2; AT1G49050.2; AT1G49050. [Q9M9A8-2]
DR GeneID; 841328; -.
DR Gramene; AT1G49050.1; AT1G49050.1; AT1G49050. [Q9M9A8-1]
DR Gramene; AT1G49050.2; AT1G49050.2; AT1G49050. [Q9M9A8-2]
DR KEGG; ath:AT1G49050; -.
DR Araport; AT1G49050; -.
DR TAIR; locus:2028466; AT1G49050.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_3_2_1; -.
DR InParanoid; Q9M9A8; -.
DR OMA; VNQKIGW; -.
DR OrthoDB; 753343at2759; -.
DR PhylomeDB; Q9M9A8; -.
DR PRO; PR:Q9M9A8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9A8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05475; nucellin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033823; Nucellin.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; PTHR13683; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aspartyl protease; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..583
FT /note="Aspartyl protease APCB1"
FT /id="PRO_0000436003"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 203..564
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT VAR_SEQ 1..201
FT /note="MEPDLHDQQQQQRVHSVVIITLPPSDDPSQGKTISAFTLTDHDYPLEIPPED
FT NPNPSFQPDPLHRNQQSRLLFSDLSMNSPRLVLGLLGISLLAVAFYASVFPNSVQMFRV
FT SPDERNRDDDDNLRETASFVFPVYHKLRAREFHERILEEDLGLENENFVESMDLELVNP
FT VKVNDVLSTSAGSIDSSTTIFPVGGNVYPDG -> MFYLQVPVLLTPPLRFFPSVVMCI
FT QMGM (in isoform 2)"
FT /id="VSP_058207"
FT MUTAGEN 223
FT /note="D->A: Loss of protease activity; when associated
FT with A-431."
FT /evidence="ECO:0000269|PubMed:26739014"
FT MUTAGEN 431
FT /note="D->A: Loss of protease activity; when associated
FT with A-223."
FT /evidence="ECO:0000269|PubMed:26739014"
SQ 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
