位置:首页 > 蛋白库 > NIP1_ARATH
NIP1_ARATH
ID   NIP1_ARATH              Reviewed;         236 AA.
AC   Q8GT75; Q8GXV3; Q9SZT2;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=NEP1-interacting protein 1;
DE   AltName: Full=RING-H2 finger protein ATL26;
GN   Name=NIP1; Synonyms=ATL26; OrderedLocusNames=At4g35840; ORFNames=F4B14.110;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   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   [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   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   [8]
RP   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:0000250}.
CC   -!- SUBUNIT: Interacts with RPOT2. {ECO:0000269|PubMed:18567673}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA21470.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81493.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ400897; CAC81897.1; -; mRNA.
DR   EMBL; AL031986; CAA21470.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161588; CAB81493.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86579.1; -; Genomic_DNA.
DR   EMBL; AK118022; BAC42655.1; -; mRNA.
DR   EMBL; BT006221; AAP12870.1; -; mRNA.
DR   PIR; T04694; T04694.
DR   RefSeq; NP_195309.2; NM_119750.3.
DR   AlphaFoldDB; Q8GT75; -.
DR   SMR; Q8GT75; -.
DR   DIP; DIP-40179N; -.
DR   IntAct; Q8GT75; 2.
DR   PaxDb; Q8GT75; -.
DR   EnsemblPlants; AT4G35840.1; AT4G35840.1; AT4G35840.
DR   GeneID; 829738; -.
DR   Gramene; AT4G35840.1; AT4G35840.1; AT4G35840.
DR   KEGG; ath:AT4G35840; -.
DR   Araport; AT4G35840; -.
DR   TAIR; locus:2125364; AT4G35840.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_013137_2_1_1; -.
DR   InParanoid; Q8GT75; -.
DR   OMA; NEAPNIF; -.
DR   PhylomeDB; Q8GT75; -.
DR   PRO; PR:Q8GT75; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GT75; baseline and differential.
DR   Genevisible; Q8GT75; 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   Chloroplast; Membrane; Metal-binding; Plastid; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..236
FT                   /note="NEP1-interacting protein 1"
FT                   /id="PRO_0000055806"
FT   TOPO_DOM        1..44
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..78
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..104
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..236
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         191..233
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CONFLICT        185
FT                   /note="S -> F (in Ref. 1; CAC81897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="V -> G (in Ref. 1; CAC81897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="H -> P (in Ref. 1; CAC81897)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  25451 MW;  1E30900A3CB1F4B7 CRC64;
     MASSRFQSGF CPISSCPSLE NFIERIKDAC RFTLSAVLGT ILSAVLTFFF ALVGTLLGAL
     TGALIGQETE SGFIRGAAVG AISGAVFSIE VFESSLVLWK SNESRFGCLL YLIDVIVSLI
     SGRLVRERIG PAMLSAVQSQ MGAVDSTFEE LSSIFDTGGS KGLTGDLVDK IPKIKITGKN
     NLDASGNKDS CSVCLQDFQL GETVRSLPHC HHMFHLPCID NWLFRHGSCP MCRRDL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024