LAMP1_ARATH
ID LAMP1_ARATH Reviewed; 681 AA.
AC Q7Y228;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable glutamate carboxypeptidase LAMP1 {ECO:0000305};
DE EC=3.4.17.21 {ECO:0000305};
DE AltName: Full=Protein LIKE AMP1 {ECO:0000303|PubMed:25673776};
GN Name=LAMP1 {ECO:0000303|PubMed:25673776};
GN OrderedLocusNames=At5g19740 {ECO:0000312|Araport:AT5G19740};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 FUNCTION.
RX PubMed=25673776; DOI=10.1104/pp.114.254623;
RA Huang W., Pitorre D., Poretska O., Marizzi C., Winter N., Poppenberger B.,
RA Sieberer T.;
RT "ALTERED MERISTEM PROGRAM1 suppresses ectopic stem cell niche formation in
RT the shoot apical meristem in a largely cytokinin-independent manner.";
RL Plant Physiol. 167:1471-1486(2015).
CC -!- FUNCTION: Acts in association with AMP1 to suppress ectopic stem cell
CC niche formation in the shoot apical meristem (SAM) independently of
CC cytokinin signaling pathway. {ECO:0000269|PubMed:25673776}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:25673776}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92744.1; -; Genomic_DNA.
DR EMBL; BT008323; AAP37682.1; -; mRNA.
DR RefSeq; NP_197475.2; NM_121979.4.
DR AlphaFoldDB; Q7Y228; -.
DR SMR; Q7Y228; -.
DR STRING; 3702.AT5G19740.1; -.
DR MEROPS; M28.A02; -.
DR PaxDb; Q7Y228; -.
DR PRIDE; Q7Y228; -.
DR ProteomicsDB; 237071; -.
DR EnsemblPlants; AT5G19740.1; AT5G19740.1; AT5G19740.
DR GeneID; 832094; -.
DR Gramene; AT5G19740.1; AT5G19740.1; AT5G19740.
DR KEGG; ath:AT5G19740; -.
DR Araport; AT5G19740; -.
DR TAIR; locus:2183229; AT5G19740.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_3_1_1; -.
DR InParanoid; Q7Y228; -.
DR OMA; VFAPGIW; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q7Y228; -.
DR PRO; PR:Q7Y228; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q7Y228; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010073; P:meristem maintenance; IGI:TAIR.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Endoplasmic reticulum; Glycoprotein;
KW Growth regulation; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..681
FT /note="Probable glutamate carboxypeptidase LAMP1"
FT /id="PRO_0000439194"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..681
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 241..527
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 681 AA; 74739 MW; 1CB394D8FF153258 CRC64;
MSKSKSLAFV IAALSYSFFS LFSSPPKSHY HELFISTSFS DNASVALNLH TLTRRPHVAG
TVANAEAAEY VRSVFTSSAL KSHVVAYQVS LTYPVHRSLV LTPTDSAKPI TFLLEQEKLG
DNPYANEVMP TFHGYAKSGN VSGPVVYANY GRVEDFVRLK KDMGVNVSGA VVIARYGQIY
RGDIVKNAYE AGAVGVVIYT DKRDYGGDEW FPASKWMPPS GVQVGTVYNG LGDPTTPGWA
SVDGCERLSD EAVELSGDVP LIPSLPVSAA DAEVILKTVV GDVSDGDVYP VGPGPGVLNL
SYIGETVIAK IENVIGVIEG EEEPDRYVIL GNHRDAWTFG AVDPNSGTAV LMEIAQRLDK
LQKRGWKPRR TIILCNWDAE EYGLIGSTEW VEENREMLSS RAVAYLNVDC AVSGPGFHAS
ATPQLDELIK VAAQEVRDPD NATQTIYESW IGSSDSVVIR RLGGGGSDYA SFVQHVGVPG
VDMSFGRGYP VYHSMYDDFT WMEKFGDPMF QRHVAMASVL GLVALRLADE EIIPFNYTSY
ALELKKSAED LENEKLGHNI DVSTLIKSIE DLSTAAKHIS LEKEAIKGAL KVRELNDRLM
MAERALTDRD GLSERPWYKH LIYGPSKYDD YGSKSFPGVD DAIDNAKKLN TKASWENVQH
QIWRVSRAIR HASLVLKGEL I
