TDC1_CAEEL
ID TDC1_CAEEL Reviewed; 705 AA.
AC Q95ZS2; Q21087;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tyrosine decarboxylase {ECO:0000312|WormBase:K01C8.3b};
DE EC=4.1.1.25 {ECO:0000305};
GN Name=tdc-1 {ECO:0000312|WormBase:K01C8.3b};
GN ORFNames=K01C8.3 {ECO:0000312|WormBase:K01C8.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15848803; DOI=10.1016/j.neuron.2005.02.024;
RA Alkema M.J., Hunter-Ensor M., Ringstad N., Horvitz H.R.;
RT "Tyramine functions independently of octopamine in the Caenorhabditis
RT elegans nervous system.";
RL Neuron 46:247-260(2005).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=25723162; DOI=10.1016/j.cell.2015.02.004;
RA Burkewitz K., Morantte I., Weir H.J., Yeo R., Zhang Y., Huynh F.K.,
RA Ilkayeva O.R., Hirschey M.D., Grant A.R., Mair W.B.;
RT "Neuronal CRTC-1 governs systemic mitochondrial metabolism and lifespan via
RT a catecholamine signal.";
RL Cell 160:842-855(2015).
CC -!- FUNCTION: Required for the decarboxylation of tyrosine to tyramine, a
CC precursor of octopamine but probably also itself a neurotransmitter
CC (PubMed:15848803). Involved in the regulation of egg laying, which is
CC inhibited by tyramine (PubMed:15848803). Also involved in controlling
CC locomotion and head movements (PubMed:15848803). Due to its involvement
CC in octopamine biosynthesis, also required for crtc-1-dependent
CC regulation of AMPK-mediated longevity which requires octopamine
CC signaling (PubMed:25723162). {ECO:0000269|PubMed:15848803,
CC ECO:0000269|PubMed:25723162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:327995; EC=4.1.1.25;
CC Evidence={ECO:0000305|PubMed:15848803};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|RuleBase:RU000382};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15848803}. Cell
CC projection, axon {ECO:0000269|PubMed:15848803}. Perikaryon
CC {ECO:0000269|PubMed:15848803}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:K01C8.3b};
CC IsoId=Q95ZS2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K01C8.3a};
CC IsoId=Q95ZS2-2; Sequence=VSP_057753, VSP_057754;
CC -!- TISSUE SPECIFICITY: Expressed in the gonadal sheath projections in
CC between the oocytes, in head RIM motor neurons and RIC interneurons.
CC {ECO:0000269|PubMed:15848803}.
CC -!- DEVELOPMENTAL STAGE: Expressed in UV1 uterine cells in late L4 larval
CC stage. {ECO:0000269|PubMed:15848803}.
CC -!- DISRUPTION PHENOTYPE: Mutants almost completely lack tyramine, have
CC fewer eggs in the uterus and are hyperactive in egg laying in the
CC presence of food with most eggs being laid at the 1-8 cell stage. They
CC also have a reduced backing response, show more spontaneous reversals
CC and fail to suppress head oscillations upon anterior touch.
CC {ECO:0000269|PubMed:15848803}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000255|RuleBase:RU000382}.
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DR EMBL; BX284602; CAA88862.1; -; Genomic_DNA.
DR EMBL; BX284602; CAC42319.1; -; Genomic_DNA.
DR PIR; T23168; T23168.
DR PIR; T23175; T23175.
DR RefSeq; NP_495743.1; NM_063342.3. [Q95ZS2-1]
DR RefSeq; NP_495744.1; NM_063343.3. [Q95ZS2-2]
DR AlphaFoldDB; Q95ZS2; -.
DR SMR; Q95ZS2; -.
DR STRING; 6239.K01C8.3b; -.
DR EPD; Q95ZS2; -.
DR PaxDb; Q95ZS2; -.
DR PeptideAtlas; Q95ZS2; -.
DR PRIDE; Q95ZS2; -.
DR EnsemblMetazoa; K01C8.3a.1; K01C8.3a.1; WBGene00006562. [Q95ZS2-2]
DR EnsemblMetazoa; K01C8.3b.1; K01C8.3b.1; WBGene00006562. [Q95ZS2-1]
DR GeneID; 174327; -.
DR KEGG; cel:CELE_K01C8.3; -.
DR UCSC; K01C8.3a; c. elegans.
DR CTD; 174327; -.
DR WormBase; K01C8.3a; CE21011; WBGene00006562; tdc-1. [Q95ZS2-2]
DR WormBase; K01C8.3b; CE28344; WBGene00006562; tdc-1. [Q95ZS2-1]
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000174368; -.
DR InParanoid; Q95ZS2; -.
DR OMA; NAIQEDR; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; Q95ZS2; -.
DR PRO; PR:Q95ZS2; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006562; Expressed in adult organism and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IMP:WormBase.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006589; P:octopamine biosynthetic process; IMP:WormBase.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..705
FT /note="Tyrosine decarboxylase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433367"
FT REGION 22..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 554..620
FT /evidence="ECO:0000255"
FT COMPBIAS 22..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 623..650
FT /note="SFLVRMVSDPKCYNPKIVRHLNMANHRK -> YTPQPLDLALAPDSDPELSP
FT CSPQILVS (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057753"
FT VAR_SEQ 651..705
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057754"
SQ SEQUENCE 705 AA; 79711 MW; B8BBDFD83582FEC6 CRC64;
MVYGLGEALK NLNSYCQERT TRIRNSLSPS RPSMSEATAT GSSSSSRAST TIPSTPNMDV
TPTVEDPRQN DNNASGMTRD EFRQYGKETV DYIVDYLENI QKRRVVPAIE PGYLKDLIPS
EAPNTPESFE SVMEDFEKLI MPGITHWQHP RFHAYFPAGN SFPSIIADML SDAIGCVGFS
WAACPAMTEL ELIMLDWFGK MIGLPAEFLP LTENGKGGGV IQSSASECNF VTLLAARFEV
MKELRQRFPF VEEGLLLSKL IAYCSKEAHS SVEKACMIGM VKLRILETDS KFRLRGDTLR
NAIQEDRNLG LIPFFVSTTL GTTSCCSFDV LSEIGPICKE NELWLHVDAA YSGSAFICPE
FRPLMNGIEY AMSFNTNPNK WLLINFDCST MWVRDRFKLT QALVVDPLYL QHSWMDKSID
YRHWGIPLSR RFRSLKLWFV IRMYGIDGLQ KYIREHVRLA KKMETLLRAD AKFEIVNEVI
MGLVCFRMKG DDELNQTLLT RLNASGRIHM VPASLGDRFV IRFCVCAENA TDKDIEVAYE
IIAQATQHVL HDSVKAVIAE EDEEAVALEE MVADLNITET PEKCLTRQNS ANAAESGQKL
ERQLSKEEIL AQKQHESLAK KRSFLVRMVS DPKCYNPKIV RHLNMANHRK MSQDLYRDRT
LMQTISHSQR PNRLSQSPGS AGSAFFDDDD DRIVADVQTG LQTPI
