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TXD15_RAT
ID   TXD15_RAT               Reviewed;         343 AA.
AC   Q5BJT4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Thioredoxin domain-containing protein 15;
DE   Flags: Precursor;
GN   Name=Txndc15;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling.
CC       Required for cilia biogenesis. {ECO:0000250|UniProtKB:Q6P6J9}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000250|UniProtKB:Q6P6J9}; Single-pass type I membrane protein
CC       {ECO:0000255}.
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DR   EMBL; BC091340; AAH91340.1; -; mRNA.
DR   RefSeq; NP_001020169.1; NM_001024998.1.
DR   AlphaFoldDB; Q5BJT4; -.
DR   SMR; Q5BJT4; -.
DR   STRING; 10116.ENSRNOP00000000146; -.
DR   GlyGen; Q5BJT4; 4 sites.
DR   PhosphoSitePlus; Q5BJT4; -.
DR   jPOST; Q5BJT4; -.
DR   PaxDb; Q5BJT4; -.
DR   PRIDE; Q5BJT4; -.
DR   Ensembl; ENSRNOT00000000146; ENSRNOP00000000146; ENSRNOG00000000133.
DR   GeneID; 307180; -.
DR   KEGG; rno:307180; -.
DR   UCSC; RGD:1304696; rat.
DR   CTD; 79770; -.
DR   RGD; 1304696; Txndc15.
DR   eggNOG; KOG2640; Eukaryota.
DR   GeneTree; ENSGT00390000002845; -.
DR   HOGENOM; CLU_050221_0_0_1; -.
DR   InParanoid; Q5BJT4; -.
DR   OMA; TCEERNV; -.
DR   OrthoDB; 1057290at2759; -.
DR   PhylomeDB; Q5BJT4; -.
DR   PRO; PR:Q5BJT4; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000000133; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q5BJT4; RN.
DR   GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR042418; TXNDC15.
DR   PANTHER; PTHR14684; PTHR14684; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cilium biogenesis/degradation;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..343
FT                   /note="Thioredoxin domain-containing protein 15"
FT                   /id="PRO_0000296096"
FT   TOPO_DOM        21..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          162..279
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          86..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   343 AA;  37928 MW;  79890F8D3A365961 CRC64;
     MQLLCWWQIL LWVLGLPARG LEEDSGHTWQ EERPVPALQV GSVYLNEEEA AQGHRVQARV
     AEPSEASLGP RGDPMVVLSV IPGAAEDQRS TEAHDGTCSA QGDEDPRCGG RENLFGLQGA
     GGFQDREEEY YAEPGVAEAE PVATEDANST DSLKSPKVNC EERNVTGLEN FTLKILNMSQ
     DLMDFLNPNG SDCTLVLFYT PWCRFSASLA PHFNSLPRAF PTLGFLALDA SQHSSLSTRF
     GTVAVPNILL FQGAKPMARF NHTDRTLETL KIFIFNQTGI EAKKNVVVTQ ADQLGPLPST
     LVKTVDWLLV FSLFFLISFI MYATIRTESI RWLIPGQEQE HAE
 
 
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