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Database: UniProt/SWISS-PROT
Entry: TPIS_CANFA
LinkDB: TPIS_CANFA
Original site: TPIS_CANFA 
ID   TPIS_CANFA              Reviewed;         249 AA.
AC   P54714;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-APR-2013, entry version 87.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=TPI1;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Beagle; TISSUE=Cornea;
RA   Wistow G.;
RT   "NEIBank analysis of dog cornea.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 8-12.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of
RT   dog heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
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DR   EMBL; DN870474; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001183983.1; NM_001197054.1.
DR   ProteinModelPortal; P54714; -.
DR   SMR; P54714; 3-249.
DR   STRING; 9615.ENSCAFP00000021462; -.
DR   UCD-2DPAGE; P54714; -.
DR   PaxDb; P54714; -.
DR   PRIDE; P54714; -.
DR   GeneID; 477711; -.
DR   KEGG; cfa:477711; -.
DR   CTD; 7167; -.
DR   eggNOG; COG0149; -.
DR   HOGENOM; HOG000226413; -.
DR   HOVERGEN; HBG002599; -.
DR   InParanoid; P54714; -.
DR   KO; K01803; -.
DR   OrthoDB; EOG40S0GF; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   NextBio; 20853140; -.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0009790; P:embryo development; IEA:Compara.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IEA:Compara.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triophos_ismrse; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Direct protein sequencing;
KW   Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    249       Triosephosphate isomerase.
FT                                /FTId=PRO_0000090112.
FT   ACT_SITE     96     96       Electrophile (By similarity).
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES     194    194       N6-acetyllysine (By similarity).
FT   MOD_RES     238    238       N6-acetyllysine (By similarity).
FT   CONFLICT     11     11       G -> N (in Ref. 2; AA sequence).
SQ   SEQUENCE   249 AA;  26715 MW;  0EF16036CD17173A CRC64;
     MAPSRKFFVG GNWKMNGRKK NLGELITTLN AAKVPADTEV VCAPPTAYID FARQKLDAKI
     AVAAQNCYKV TNGAFTGEIS PGMIKDCGAT WVVLGHSERR HVFGESDELI GQKVAHALAE
     GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ
     QAQEVHEKLR GWLKSNVSDA VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE
     FVDIINAKQ
//
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