ID S9YMJ8_CAMFR Unreviewed; 629 AA.
AC S9YMJ8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pre-mRNA-splicing regulator WTAP {ECO:0000256|ARBA:ARBA00017540};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE AltName: Full=Female-lethal(2)D homolog {ECO:0000256|ARBA:ARBA00033097};
DE AltName: Full=WT1-associated protein {ECO:0000256|ARBA:ARBA00032703};
DE AltName: Full=Wilms tumor 1-associating protein {ECO:0000256|ARBA:ARBA00032336};
GN ORFNames=CB1_000390054 {ECO:0000313|EMBL:EPY85240.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY85240.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY85240.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the fl(2)d family.
CC {ECO:0000256|ARBA:ARBA00010313}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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DR EMBL; KB016679; EPY85240.1; -; Genomic_DNA.
DR AlphaFoldDB; S9YMJ8; -.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0080009; P:mRNA methylation; IEA:InterPro.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR InterPro; IPR033757; WTAP.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR Pfam; PF17098; Wtap; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW Transferase {ECO:0000313|EMBL:EPY85240.1}.
FT DOMAIN 248..499
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 506..628
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 94..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 66428 MW; B7890B303C90C5BA CRC64;
MDMLRKRRCQ TGKKLMAKCR MLIQENQELG RQLSQGRIAQ LEAELALQKK YSEELKSSQD
ELNDFIIQLD EEVEGMQSTI LVLQQQLKET RQQLAQYQQQ QSQAPGPSTS RTASSEPVGQ
AEAAGKDCSR LANGPSNGSS SRQRTSGSGF HREGDTTEDD FPSSPGNGNK ASSSSEERTG
RGGSSYVNQL SAGYESVDSP TGSENSLTHH SNDTDSSHDP QEEKTVSGKV RRPAATLGAL
SIALAFASVL GSFNGALSTV PVHDLGSTVI REVLKRAAVA PEEVSEVIFG HVLAAGCGQN
PVRQASVGAG IPYSVPAWSC QMLCGSGLKA VCLAAQSIGI GDSSIVVAGG MESMSKAPHL
VHLRTGVKIG ETALTDSILC DGLTDAFHNY HMGITAENVA KKWQVSREDQ DKVAVLSQNR
TENAQKAGHF DKEIVSVFVS SRKGLTEVKT DEFPRHGSNI EDMSKLKPYF LTDGTGTVTA
ANASGINDGA AAVVLMKQSE ATNRGLKPLA QIVSWSQAGV EPSIMGTGPI PAIKQAVAKA
GWSLEDVDVF EINEAFAAVS AAITKELGLN PEKVNTEGGA IALGHPLGAS GCRILVTLLH
TMERKGGRRG VAALCVGGGM GIAMCVQRA
//
