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NET2A_ARATH
ID   NET2A_ARATH             Reviewed;         947 AA.
AC   P0DMS1; Q9C6Q9;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Protein NETWORKED 2A {ECO:0000303|PubMed:22840520};
GN   Name=NET2A {ECO:0000303|PubMed:22840520};
GN   OrderedLocusNames=At1g58215 {ECO:0000312|Araport:AT1G58215};
GN   ORFNames=T18I24.12 {ECO:0000312|EMBL:AAG50760.1};
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   FUNCTION, DOMAIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY,
RP   AND NOMENCLATURE.
RX   PubMed=22840520; DOI=10.1016/j.cub.2012.06.041;
RA   Deeks M.J., Calcutt J.R., Ingle E.K., Hawkins T.J., Chapman S.,
RA   Richardson A.C., Mentlak D.A., Dixon M.R., Cartwright F., Smertenko A.P.,
RA   Oparka K., Hussey P.J.;
RT   "A superfamily of actin-binding proteins at the actin-membrane nexus of
RT   higher plants.";
RL   Curr. Biol. 22:1595-1600(2012).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=24926301; DOI=10.3389/fpls.2014.00254;
RA   Hawkins T.J., Deeks M.J., Wang P., Hussey P.J.;
RT   "The evolution of the actin binding NET superfamily.";
RL   Front. Plant Sci. 5:254-254(2014).
CC   -!- FUNCTION: Plant-specific actin binding protein. Associates with F-actin
CC       at the plasma membrane in growing pollen tubes. May be part of a
CC       membrane-cytoskeletal adapter complex. {ECO:0000269|PubMed:22840520}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22840520}.
CC       Note=In growing pollen tubes, forms foci at the plasma membrane, but
CC       not at the pollen tube tip. {ECO:0000269|PubMed:22840520}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in pollen.
CC       {ECO:0000269|PubMed:22840520}.
CC   -!- DOMAIN: The NAB domain, also called NAB (NET actin-binding) domain, is
CC       sufficient for F-actin binding. {ECO:0000269|PubMed:22840520}.
CC   -!- SIMILARITY: Belongs to the NET family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG50760.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g58210 has been split into 2 genes: At1g58210 and At1g58215.; Evidence={ECO:0000305};
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DR   EMBL; AC079131; AAG50760.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; ANM59275.1; -; Genomic_DNA.
DR   RefSeq; NP_001321645.1; NM_001333822.1.
DR   AlphaFoldDB; P0DMS1; -.
DR   SMR; P0DMS1; -.
DR   STRING; 3702.AT1G58210.1; -.
DR   PaxDb; P0DMS1; -.
DR   PRIDE; P0DMS1; -.
DR   ProteomicsDB; 250589; -.
DR   EnsemblPlants; AT1G58215.1; AT1G58215.1; AT1G58215.
DR   GeneID; 842188; -.
DR   Gramene; AT1G58215.1; AT1G58215.1; AT1G58215.
DR   KEGG; ath:AT1G58215; -.
DR   Araport; AT1G58215; -.
DR   eggNOG; ENOG502QQVH; Eukaryota.
DR   OMA; HEMNGLK; -.
DR   OrthoDB; 186795at2759; -.
DR   PRO; PR:P0DMS1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P0DMS1; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   InterPro; IPR011684; NAB.
DR   Pfam; PF07765; KIP1; 1.
DR   PROSITE; PS51774; NAB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Membrane; Reference proteome.
FT   CHAIN           1..947
FT                   /note="Protein NETWORKED 2A"
FT                   /id="PRO_0000431853"
FT   DOMAIN          10..90
FT                   /note="NAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01110"
FT   REGION          105..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          348..454
FT                   /evidence="ECO:0000255"
FT   COILED          568..619
FT                   /evidence="ECO:0000255"
FT   COILED          722..809
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        620..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  108032 MW;  56BB435AE3119025 CRC64;
     MLQRAASNAY SWWWASHIRT KQSKWLEHNL QDMEEKVEYT LKIIDEDGDT FAKRAEMYYR
     KRPEIVNFVE EAFRSYRALA ERYDHLSREL QSANRTIATA FPEHVQFPLE DDSDENEDYD
     GRPRKPPKHL HLIPKGINIP EVPDIPKKKD FRSQSMMLSR KGPADLKRNV SSAQAKREAA
     IVRSGLSKEE GLEEIDKLQK GILALQTEKE FVRSSYEESY ERYWDLENEV TEMQKSVCNL
     QDEFGLGASI DDSDARTLMA STALSSCRDT LAKLEEKQKI SIEEAEIEKG RITTAKERFY
     ALRNKFEKPE SDVLDEVIRT DEEEEDVVQE SSYESEREDS NENLTVVKLA EKIDDLVHRV
     VSLETNASSH TALVKTLRSE TDELHEHIRG LEEDKAALVS DATVMKQRIT VLEDELRNVR
     KLFQKVEDQN KNLQNQFKVA NRTVDDLSGK IQDVKMDEDV EGAGIFQELP VVSGSEDSRD
     DLKSVSTEKT KKDVIAVKES EDGERAQEEK PEIKDSFALS ETASTCFGTE AEDLVTEDED
     EETPNWRHLL PDGMEDREKV LLDEYTSVLR DYREVKRKLG DVEKKNREGF FELALQLREL
     KNAVAYKDVE IQSLRQKLDT TGKDSPHQGE GNNQLEHEQG HHETVSISPT SNFSVATTPH
     HQVGDVKRTP GRTKSTEVRV KFADVDDSPR TKIPTVEDKV RADIDAVLEE NLEFWLRFST
     SVHQIQKYQT TVQDLKSELS KLRIESKQQQ ESPRSSSNTA VASEAKPIYR HLREIRTELQ
     LWLENSAVLK DELQGRYASL ANIQEEIARV TAQSGGNKVS DSEISGYQAA KFHGEILNMK
     QENKRVSTEL HSGLDRVRAL KTEVERILSK LEEDLGISSA TEARTTPSKS SSSGRPRIPL
     RSFLFGVKLK KNRQQKQSAS SLFSCVSPSP GLHKQSSYSR PPGKLPE
 
 
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