ID   UBP14_ARATH             Reviewed;         797 AA.
AC   Q8L6Y1; Q0WV77; Q9FPT0; Q9LJT6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE            EC=3.1.2.15;
DE   AltName: Full=Ubiquitin thioesterase 14;
DE   AltName: Full=Ubiquitin-specific-processing protease 14;
DE   AltName: Full=Deubiquitinating enzyme 14;
DE            Short=AtUBP14;
DE   AltName: Full=TITAN-6 protein;
GN   Name=UBP14; Synonyms=TTN6; OrderedLocusNames=At3g20630, At3g20625;
GN   ORFNames=F3H11_1, K10D20.17, K10D20.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20567829; PubMed=11115897; DOI=10.1104/pp.124.4.1828;
RA   Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.;
RT   "The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2
RT   are required for the resistance to the amino acid analog canavanine.";
RL   Plant Physiol. 124:1828-1843(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20363099; PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II.
RT   Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
RT   and BAC clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11576424; DOI=10.1046/j.1365-313X.2001.01106.x;
RA   Doelling J.H., Yan N., Kurepa J., Walker J., Vierstra R.D.;
RT   "The ubiquitin-specific protease UBP14 is essential for early embryo
RT   development in Arabidopsis thaliana.";
RL   Plant J. 27:393-405(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=11788751; DOI=10.1104/pp.128.1.38;
RA   Tzafrir I., McElver J.A., Liu C.-M., Yang L.J., Wu J.Q., Martinez A.,
RA   Patton D.A., Meinke D.W.;
RT   "Diversity of TITAN functions in Arabidopsis seed development.";
RL   Plant Physiol. 128:38-51(2002).
RN   [7]
RP   STRUCTURE BY NMR OF 594-665.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-011, a UBA domain from Arabidopsis
RT   cDNA.";
RL   Submitted (SEP-2004) to the PDB data bank.
RN   [8]
RP   STRUCTURE BY NMR OF 651-710.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-023, a UBA domain from Arabidopsis
RT   cDNA.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin precursors as well as that of ubiquinated proteins.
CC       Involved in seed and embryo development.
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- TISSUE SPECIFICITY: Constitutively and ubiquitously expressed (at
CC       protein level).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 2 UBA domains.
CC   -!- SIMILARITY: Contains 1 UBP-type zinc finger.
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DR   EMBL; AF302664; AAG42755.1; -; mRNA.
DR   EMBL; AP000410; BAB01171.1; -; Genomic_DNA.
DR   EMBL; AP002034; BAB01171.1; JOINED; Genomic_DNA.
DR   EMBL; AY140096; AAM98237.1; -; mRNA.
DR   EMBL; AK226894; BAE98971.1; -; mRNA.
DR   IPI; IPI00525815; -.
DR   RefSeq; NP_566666.2; -.
DR   UniGene; At.16942; -.
DR   PDB; 1VEK; NMR; -; A=594-664.
DR   PDB; 1WIV; NMR; -; A=651-710.
DR   PDBsum; 1VEK; -.
DR   PDBsum; 1WIV; -.
DR   SMR; Q8L6Y1; 157-272.
DR   MEROPS; C19.084; -.
DR   PRIDE; Q8L6Y1; -.
DR   GeneID; 821610; -.
DR   GenomeReviews; BA000014_GR; AT3G20630.
DR   KEGG; ath:AT3G20630; -.
DR   NMPDR; fig|3702.1.peg.14295; -.
DR   TAIR; At3g20630; -.
DR   OMA; Q8L6Y1; ERAVDWI.
DR   BRENDA; 3.1.2.15; 302.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009793; P:embryonic development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:TAIR.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Hydrolase; Metal-binding; Protease;
KW   Repeat; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    797       Ubiquitin carboxyl-terminal hydrolase 14.
FT                                /FTId=PRO_0000080697.
FT   DOMAIN      613    654       UBA 1.
FT   DOMAIN      670    710       UBA 2.
FT   ZN_FING     178    252       UBP-type.
FT   ACT_SITE    317    317       By similarity.
FT   ACT_SITE    749    749       By similarity.
FT   ACT_SITE    758    758       By similarity.
FT   CONFLICT    601    601       G -> A (in Ref. 1; AAG42755).
FT   STRAND      603    605
FT   HELIX       616    625
FT   HELIX       629    638
FT   TURN        639    641
FT   HELIX       644    654
FT   TURN        659    661
FT   HELIX       673    682
FT   HELIX       686    695
FT   HELIX       700    709
SQ   SEQUENCE   797 AA;  88374 MW;  B827C513A6D5C4E2 CRC64;
     MELLRSNLSR VQIPEPTHRI YKHECCISFD TPRSEGGLFV DMNSFLAFGK DYVSWNYEKT
     GNPVYLHIKQ TRKSIPEDRP LKKPTLLAIG VDGGFDNNEP EYEESYSIVI LPDFVSLPFP
     SVELPEKVRI AVDTVVNAVG AERKEQVAAW TAEKKLISEH ALTLQQIKSG IVIPPSGWKC
     SKCDKTENLW LNLTDGMILC GRKNWDGTGG NNHAVEHYKE TAYPLAVKLG TITADLEAAD
     VYSYPEDDSV LDPLLAEHLA HFGIDFSSMQ KTEMTTAERE LDQNTNFDWN RIQESGKELV
     PVFGPGYTGL VNLGNSCYLA ATMQIVFSTH SFISRYFSHQ SLKMAFEMAP ADPTLDLNMQ
     LTKLGHGLLS GKYSMPATQK DATTGDPRQE GIPPRMFKNV IAASHAEFSS MRQQDALDFF
     LHLVGKVERA SNTTPDLDPS RSFKFGIEEK ILCPSGKVGY NKREDCILSL NIPLHEATNK
     DELEAFHKQK AGKGLEENDM RSSDEIVRPR VPLEACLANF ASSEPIEDYY SSALKGMTTA
     IKTTGLTSFP DYLVLHMRKF VMEEGWVPKK LDVYIDVPDV IDISHMRSKG LQPGEELLPD
     GVPEEVMESA QPVANEEIVA QLVSMGFSQL HCQKAAINTS NAGVEEAMNW LLSHMDDPDI
     DAPISHQTSD IDQSSVDTLL SFGFAEDVAR KALKASGGDI EKATDWVFNN PNASVSDMDV
     SSSNSAQTPA QSGLPDGGGK YKLFGIVSHM GTSVHCGHYV AHILKEGRWV IFNDDKVGIS
     TDPPKDMGYV YFFQRLD
//