TTM2_CAEEL
ID TTM2_CAEEL Reviewed; 358 AA.
AC Q19829;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protein ttm-2 {ECO:0000305};
DE AltName: Full=Toxin-regulated target of MAPK 2 {ECO:0000312|WormBase:F26G1.4};
GN Name=ttm-2 {ECO:0000312|WormBase:F26G1.4};
GN ORFNames=F26G1.4 {ECO:0000312|WormBase:F26G1.4};
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15256590; DOI=10.1073/pnas.0404073101;
RA Huffman D.L., Abrami L., Sasik R., Corbeil J., van der Goot F.G.,
RA Aroian R.V.;
RT "Mitogen-activated protein kinase pathways defend against bacterial pore-
RT forming toxins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10995-11000(2004).
CC -!- FUNCTION: Involved in resistance to B.thuringiensis pore-forming toxin
CC Cry5B downstream of the sek-1 and pmk-1 MAPK kinase pathway.
CC {ECO:0000269|PubMed:15256590}.
CC -!- INDUCTION: By B.thuringiensis pore-forming toxin Cry5B.
CC {ECO:0000269|PubMed:15256590}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes variable
CC hypersensitivity to low, chronic doses of the B.thuringiensis pore-
CC forming toxin Cry5B but not to heavy metal Cd(2+) exposure.
CC {ECO:0000269|PubMed:15256590}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; BX284602; CCD65847.1; -; Genomic_DNA.
DR PIR; T16180; T16180.
DR RefSeq; NP_494855.1; NM_062454.1.
DR AlphaFoldDB; Q19829; -.
DR IntAct; Q19829; 1.
DR STRING; 6239.F26G1.4.1; -.
DR PaxDb; Q19829; -.
DR EnsemblMetazoa; F26G1.4.1; F26G1.4.1; WBGene00017840.
DR GeneID; 184995; -.
DR KEGG; cel:CELE_F26G1.4; -.
DR UCSC; F26G1.4; c. elegans.
DR CTD; 184995; -.
DR WormBase; F26G1.4; CE02696; WBGene00017840; ttm-2.
DR eggNOG; ENOG502TGWV; Eukaryota.
DR HOGENOM; CLU_674943_0_0_1; -.
DR InParanoid; Q19829; -.
DR OMA; FKTEYSL; -.
DR OrthoDB; 926164at2759; -.
DR PRO; PR:Q19829; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017840; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0093002; P:response to nematicide; IMP:UniProtKB.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00339; Arrestin_N; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..358
FT /note="Protein ttm-2"
FT /id="PRO_0000446894"
SQ SEQUENCE 358 AA; 40588 MW; 968EAE9CAC54E32A CRC64;
MLDKIRFTVL LDRPFYQPGQ TIQGHVVCEP HHPLEIDCVE GRLHGEIQYF QQLPPNHNRN
GSPLPPSKTR VLIDEKAQLW KYQTVSEMLG LDVFYDENQN RHFSSESASA SSSSLFTTAA
TFPIQIELPH FAPPSFYCPG SPVSIRFTLE IQLYNQGFKI ASHEENLVVL NYESIKRQVT
PKPVNFQKTF NFPKERSISL EMLLPTDVFT TTARLENCIT ICNRWKQSLK YVHLNIVRRI
SALNQNNEVI DTVKIDTTGV GLPSKTKIAV GETYSFRPTF NVPALPPNIH VNGLFKTEYS
LKVTIGRAHN FVLASYEVPI TIVTMDQSSR RSMQKEDILV DISASNNTLN NLPVDLLA
