NIP2_ARATH
ID NIP2_ARATH Reviewed; 241 AA.
AC Q8GT74; Q8GWW3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=NEP1-interacting protein 2;
DE AltName: Full=RING-H2 finger protein ATL25;
GN Name=NIP2; Synonyms=ATL25; OrderedLocusNames=At2g17730; ORFNames=T17A5.9;
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. C24;
RA Hakimi M.A., Lagrange T., Lerbs-Mache S.;
RT "Characterization of NEP-1 interacting transcription factors.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH RPOT2.
RX PubMed=18567673; DOI=10.1073/pnas.0800909105;
RA Azevedo J., Courtois F., Hakimi M.A., Demarsy E., Lagrange T.,
RA Alcaraz J.P., Jaiswal P., Marechal-Drouard L., Lerbs-Mache S.;
RT "Intraplastidial trafficking of a phage-type RNA polymerase is mediated by
RT a thylakoid RING-H2 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9123-9128(2008).
CC -!- FUNCTION: Intrinsic thylakoid membrane protein that fixes RPOT2 on the
CC stromal side of the thylakoid membrane. {ECO:0000269|PubMed:18567673}.
CC -!- SUBUNIT: Interacts with RPOT2. {ECO:0000269|PubMed:18567673}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18567673}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18567673}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GT74-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. NIP subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally assigned as a member of the E3 ubiquitin-
CC protein ligase ATL subfamily. {ECO:0000305|PubMed:16557337}.
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DR EMBL; AJ400898; CAC81898.1; -; mRNA.
DR EMBL; CP002685; AEC06675.1; -; Genomic_DNA.
DR EMBL; AK118593; BAC43193.1; -; mRNA.
DR RefSeq; NP_179364.2; NM_127327.4. [Q8GT74-1]
DR AlphaFoldDB; Q8GT74; -.
DR SMR; Q8GT74; -.
DR BioGRID; 1639; 1.
DR DIP; DIP-40180N; -.
DR IntAct; Q8GT74; 1.
DR STRING; 3702.AT2G17730.2; -.
DR PaxDb; Q8GT74; -.
DR PRIDE; Q8GT74; -.
DR EnsemblPlants; AT2G17730.1; AT2G17730.1; AT2G17730. [Q8GT74-1]
DR GeneID; 816282; -.
DR Gramene; AT2G17730.1; AT2G17730.1; AT2G17730. [Q8GT74-1]
DR KEGG; ath:AT2G17730; -.
DR Araport; AT2G17730; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_2_1_1; -.
DR InParanoid; Q8GT74; -.
DR OMA; DLWHSGD; -.
DR PhylomeDB; Q8GT74; -.
DR PRO; PR:Q8GT74; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GT74; baseline and differential.
DR Genevisible; Q8GT74; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027367; Gly-zipper_YMGG.
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; PF13441; Gly-zipper_YMGG; 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 Alternative splicing; Chloroplast; Membrane; Metal-binding; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix; Zinc;
KW Zinc-finger.
FT CHAIN 1..241
FT /note="NEP1-interacting protein 2"
FT /id="PRO_0000055776"
FT TOPO_DOM 1..36
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..76
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..241
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT ZN_FING 196..238
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 44
FT /note="G -> A (in Ref. 4; BAC43193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 25803 MW; 70855573A651B007 CRC64;
MASSSSSSYR FQSGSYPLSS SPSLGNFVER IKDACHFLVS AVLGTIISAI LTFFFALVGT
LLGALTGALI GQETESGFIR GAAIGAISGA VFSIEVFESS LDLWKSDESG FGCFLYLIDV
IVSLLSGRLV RERIGPAMLS AVQSQMGAVD TAFDDHTSLF DTGGSKGLTG DLVEKIPKMT
ITGNNNTDAS ENTDSCSVCL QDFQLGETVR SLPHCHHMFH LPCIDNWLLR HGSCPMCRRD
I
