NIPL2_ARATH
ID NIPL2_ARATH Reviewed; 223 AA.
AC Q8LBA0; Q4TU31; Q94A26; Q9CA72;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NEP1-interacting protein-like 2;
DE AltName: Full=RING-H2 finger protein ATL24;
GN Name=ATL24; OrderedLocusNames=At1g74410; ORFNames=F1M20.9;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [7]
RP FUNCTION, AND NO CATALYTIC ACTIVITY.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [8]
RP NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT "The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a
RT large number of putative ubiquitin ligases of the RING-H2 type.";
RL J. Mol. Evol. 62:434-445(2006).
RN [9]
RP INDUCTION BY CHITIN.
RX PubMed=17722694; DOI=10.1094/mpmi-20-8-0900;
RA Libault M., Wan J., Czechowski T., Udvardi M., Stacey G.;
RT "Identification of 118 Arabidopsis transcription factor and 30 ubiquitin-
RT ligase genes responding to chitin, a plant-defense elicitor.";
RL Mol. Plant Microbe Interact. 20:900-911(2007).
CC -!- FUNCTION: May be involved in the early steps of the plant defense
CC signaling pathway. Does not display E3 catalytic activity.
CC {ECO:0000269|PubMed:16339806}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by chitin. {ECO:0000269|PubMed:17722694}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. NIP subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:16557337) assigned as a member of the
CC E3 ubiquitin-protein ligase ATL subfamily but does not display E3
CC catalytic activity (PubMed:16339806). {ECO:0000305|PubMed:16339806,
CC ECO:0000305|PubMed:16557337}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52385.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ059105; AAY57591.1; -; mRNA.
DR EMBL; AC011765; AAG52385.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35588.1; -; Genomic_DNA.
DR EMBL; AY050433; AAK91449.1; -; mRNA.
DR EMBL; AY093797; AAM10413.1; -; mRNA.
DR EMBL; AY087335; AAM64885.1; -; mRNA.
DR PIR; H96772; H96772.
DR RefSeq; NP_565085.1; NM_106101.4.
DR AlphaFoldDB; Q8LBA0; -.
DR SMR; Q8LBA0; -.
DR BioGRID; 29001; 1.
DR IntAct; Q8LBA0; 1.
DR STRING; 3702.AT1G74410.1; -.
DR PaxDb; Q8LBA0; -.
DR PRIDE; Q8LBA0; -.
DR ProteomicsDB; 236830; -.
DR EnsemblPlants; AT1G74410.1; AT1G74410.1; AT1G74410.
DR GeneID; 843782; -.
DR Gramene; AT1G74410.1; AT1G74410.1; AT1G74410.
DR KEGG; ath:AT1G74410; -.
DR Araport; AT1G74410; -.
DR TAIR; locus:2019110; AT1G74410.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_2_1_1; -.
DR InParanoid; Q8LBA0; -.
DR OMA; LACVDKW; -.
DR OrthoDB; 1299803at2759; -.
DR PhylomeDB; Q8LBA0; -.
DR PRO; PR:Q8LBA0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LBA0; baseline and differential.
DR Genevisible; Q8LBA0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044523; NIP1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46151; PTHR46151; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Plant defense; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..223
FT /note="NEP1-interacting protein-like 2"
FT /id="PRO_0000055773"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 176..218
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 121
FT /note="M -> I (in Ref. 5; AAM64885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24262 MW; 700187C970623CC0 CRC64;
MDTTLSPAVE AEQIADSTID TVSRLIAGVF SGALTGIFAM AGAFTGAVTG AVAGRAAQYG
VLRGAALGAV AGAILSVEVL EASRAYWYLE LSGSRGPSSM ADFVEQLFRG RLVDEQLMST
MINSHHWQLR ISDVSYEERE DVYGELEARG LSGDSLRKLP CYIMSSEMVR RQVTHCTICL
QDIKTGEITR SLPKCDHTFH LVCVDKWLIR HGSCPICRQA VKD
