C3H16_ARATH
ID C3H16_ARATH Reviewed; 435 AA.
AC Q9FWS3; F4HZ22; Q94C30;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Zinc finger CCCH domain-containing protein 16;
DE Short=AtC3H16;
GN Name=CG1 {ECO:0000303|PubMed:21189294};
GN OrderedLocusNames=At1g75340 {ECO:0000312|Araport:AT1G75340};
GN ORFNames=F1B16.12 {ECO:0000312|EMBL:AAG13074.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-435.
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 NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [5]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT "Identification and characterization of nuclear pore complex components in
RT Arabidopsis thaliana.";
RL Plant Cell 22:4084-4097(2010).
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC fold symmetrical structure comprising a central transport channel and
CC two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC are attached. The cytoplasmic filaments have loose ends, while the
CC nuclear filaments are joined in a distal ring, forming a nuclear
CC basket. NPCs are highly dynamic in configuration and composition, and
CC can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC subcomplex and the NUP93 subcomplex, containing approximately 30
CC different nucleoporin proteins. {ECO:0000305|PubMed:21189294}.
CC -!- INTERACTION:
CC Q9FWS3; Q9XFM0: IAA28; NbExp=3; IntAct=EBI-25527280, EBI-3133404;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21189294}.
CC Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FWS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FWS3-2; Sequence=VSP_057130, VSP_057131;
CC -!- DOMAIN: Contains FG repeats mediating the translocation through the NPC
CC by interacting with transport factors. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2]: Derived from proteomic data. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK59780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC023754; AAG13074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35703.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35704.1; -; Genomic_DNA.
DR EMBL; AY037195; AAK59780.1; ALT_INIT; mRNA.
DR EMBL; BT004555; AAO42801.1; -; mRNA.
DR PIR; H96783; H96783.
DR RefSeq; NP_001185401.1; NM_001198472.1. [Q9FWS3-2]
DR RefSeq; NP_565108.2; NM_106188.3. [Q9FWS3-1]
DR AlphaFoldDB; Q9FWS3; -.
DR SMR; Q9FWS3; -.
DR BioGRID; 29089; 25.
DR IntAct; Q9FWS3; 1.
DR STRING; 3702.AT1G75340.1; -.
DR PaxDb; Q9FWS3; -.
DR PRIDE; Q9FWS3; -.
DR DNASU; 843870; -.
DR EnsemblPlants; AT1G75340.1; AT1G75340.1; AT1G75340. [Q9FWS3-1]
DR EnsemblPlants; AT1G75340.2; AT1G75340.2; AT1G75340. [Q9FWS3-2]
DR GeneID; 843870; -.
DR Gramene; AT1G75340.1; AT1G75340.1; AT1G75340. [Q9FWS3-1]
DR Gramene; AT1G75340.2; AT1G75340.2; AT1G75340. [Q9FWS3-2]
DR KEGG; ath:AT1G75340; -.
DR Araport; AT1G75340; -.
DR TAIR; locus:2018452; AT1G75340.
DR eggNOG; ENOG502QVMW; Eukaryota.
DR InParanoid; Q9FWS3; -.
DR OMA; NKWTRSS; -.
DR OrthoDB; 1562631at2759; -.
DR PhylomeDB; Q9FWS3; -.
DR PRO; PR:Q9FWS3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWS3; baseline and differential.
DR Genevisible; Q9FWS3; AT.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11224; PTHR11224; 2.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Translocation; Transport; Zinc; Zinc-finger.
FT CHAIN 1..435
FT /note="Zinc finger CCCH domain-containing protein 16"
FT /id="PRO_0000371975"
FT REPEAT 34..35
FT /note="1"
FT REPEAT 36..37
FT /note="2"
FT REPEAT 56..57
FT /note="3"
FT REPEAT 58..59
FT /note="4"
FT REPEAT 343..344
FT /note="5"
FT REPEAT 359..360
FT /note="6"
FT ZN_FING 1..27
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 2..88
FT /note="6 X 2 AA repeats of F-G"
FT REGION 25..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 13
FT /note="S -> SLGFVFYILGFNLKSIDVRRC (in isoform 2)"
FT /id="VSP_057130"
FT VAR_SEQ 226..282
FT /note="Missing (in isoform 2)"
FT /id="VSP_057131"
SQ SEQUENCE 435 AA; 46798 MW; 4E722A78880E21F6 CRC64;
MRKELCRNFQ RGSCRYGENC RFLHPQQAKP NNPFGFGTQN QQQQQQQQQQ NSSNPFGFGV
QSGGSSRPNQ FQNTWSRTAS TPTGGGAAAS TQQTGKQTQP ADHKCTDPAA CKRVMQDDFK
NERPMWKLTC YGHWKYFPCD VTGDISYEEL RAVAYEEAKR GIPLQSIVER ERNLQNSKIA
EFENFLRNPY KGSVTANQSP FAATTPSIFP QSSQINSPSP AFSGFNQQTA FSNTNAGGLS
SSGPPNAFAS FNQQTTFPNT NAGGVSSSGP PNPFASFTQQ SNNQQTAFSN TNAGGLSSSG
PPNAFASFNK QPNAFSVNTP QPVPSGPSGF QTNPSTTFKP ASFGPGPGFA TTPQNNNIFG
QSTPTPATNT SQNNQTAFNF NVPVASFTAP AINTTNTSSG TELQIGGDPV DSSIWLKEKW
NPGEIPEQAP PDAFV
