LOCUS       NP_001010946             458 aa            linear   ROD 02-JUN-2024
DEFINITION  protein adenylyltransferase FICD [Rattus norvegicus].
ACCESSION   NP_001010946 XP_222280
VERSION     NP_001010946.1
DBSOURCE    REFSEQ: accession NM_001010946.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Sanyal,A., Chen,A.J., Nakayasu,E.S., Lazar,C.S., Zbornik,E.A.,
            Worby,C.A., Koller,A. and Mattoo,S.
  TITLE     A novel link between Fic (filamentation induced by cAMP)-mediated
            adenylylation/AMPylation and the unfolded protein response
  JOURNAL   J Biol Chem 290 (13), 8482-8499 (2015)
   PUBMED   25601083
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Bunney,T.D., Cole,A.R., Broncel,M., Esposito,D., Tate,E.W. and
            Katan,M.
  TITLE     Crystal structure of the human, FIC-domain containing protein HYPE
            and implications for its functions
  JOURNAL   Structure 22 (12), 1831-1843 (2014)
   PUBMED   25435325
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Engel,P., Goepfert,A., Stanger,F.V., Harms,A., Schmidt,A.,
            Schirmer,T. and Dehio,C.
  TITLE     Adenylylation control by intra- or intermolecular active-site
            obstruction in Fic proteins
  JOURNAL   Nature 482 (7383), 107-110 (2012)
   PUBMED   22266942
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Worby,C.A., Mattoo,S., Kruger,R.P., Corbeil,L.B., Koller,A.,
            Mendez,J.C., Zekarias,B., Lazar,C. and Dixon,J.E.
  TITLE     The fic domain: regulation of cell signaling by adenylylation
  JOURNAL   Mol Cell 34 (1), 93-103 (2009)
   PUBMED   19362538
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079197.1.
            
            On Jan 28, 2005 this sequence version replaced XP_222280.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079197.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..458
                     /product="protein adenylyltransferase FICD"
                     /EC_number="2.7.7.108"
                     /note="adenosine monophosphate-protein transferase FICD;
                     huntingtin interactor protein E; AMPylator FICD; FIC
                     domain-containing protein; de-AMPylase FICD; FIC domain
                     containing"
                     /calculated_mol_wt=51623
     Site            24..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY47.1)"
     Region          <105..>184
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          106..139
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY47.1)"
     Region          106..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(107,110..111,114..115,117,141,144..145,148..149,
                     151..152,175,178..179,182..183,186)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          139..169
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          140..173
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY47.1)"
     Region          181..>423
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
     Region          230..235
                     /region_name="Inhibitory (S/T)XXXE(G/N) motif.
                     /evidence=ECO:0000250|UniProtKB:Q9BVA6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY47.1)"
     Site            234
                     /site_type="other"
                     /note="Important for autoinhibition of adenylyltransferase
                     activity. /evidence=ECO:0000250|UniProtKB:Q9BVA6;
                     propagated from UniProtKB/Swiss-Prot (Q6AY47.1)"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY47.1)"
     CDS             1..458
                     /gene="Ficd"
                     /coded_by="NM_001010946.1:404..1780"
                     /db_xref="GeneID:288741"
                     /db_xref="RGD:1359391"
ORIGIN      
        1 milmpmasvv avaepkwvsv wgrflwmtll smalgsllal llplgaveeq clavlrgfhl
       61 lrskldraqh vvtkctspst elsvtsrdag lltvktkasp agkleakaal nqalemkrqg
      121 krgkahklfl halkmdpgfv dalnelgifs eedkdiiqad ylytraltis pfhekalinr
      181 drtlplveei dqryfsvlds kvrkvmsipk gssalrrvme etyyhhiyht vaiegntltl
      241 aeirhiletr yavpgkslee qnevigmhaa mkyinstlvs rigsvtidhm leihrrvlgy
      301 vdpveagrfr rtqvlvghhi pphprdvekq mqeftqwlns edamnlhpve faalahyklv
      361 yihpfidgng rtsrllmnli lmqagyppit irkeqrseyy hvlevanegd vrpfirfiak
      421 ctevtldtll latteysaal peaqpnhsgf ketlpvrp
//
