ID   IFT57_BOVIN             Reviewed;         429 AA.
AC   Q5EA95;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Intraflagellar transport protein 57 homolog;
GN   Name=IFT57;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11916979; DOI=10.1083/jcb.200107108;
RA   Pazour G.J., Baker S.A., Deane J.A., Cole D.G., Dickert B.L.,
RA   Rosenbaum J.L., Witman G.B., Besharse J.C.;
RT   "The intraflagellar transport protein, IFT88, is essential for vertebrate
RT   photoreceptor assembly and maintenance.";
RL   J. Cell Biol. 157:103-113(2002).
CC   -!- FUNCTION: Required for the formation of cilia. Plays an indirect role
CC       in sonic hedgehog signaling, cilia being required for all activity of
CC       the hedgehog pathway. Has pro-apoptotic function via its interaction
CC       with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis.
CC       Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in
CC       the promoter of caspase genes such as CASP1, CASP8 and CASP10,
CC       suggesting that it may act as a transcription regulator; however the
CC       relevance of such function remains unclear (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC       IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC       IFT80, IFT81, and IFT88 (By similarity). Interacts with IFT20 (By
CC       similarity). Interacts with IFT88 (By similarity). Interacts with
CC       IFT80, IFT-81, IFT74, IFT172, TTC30B and KIF17 (By similarity).
CC       Interacts with BLOC1S2 (By similarity). Interacts with RYBP (By
CC       similarity). Interacts with HOMER1; the interaction possibly prevents
CC       the pro-apoptotic effects of IFT57 (By similarity). Interacts with HIP1
CC       (By similarity). In normal conditions, it poorly interacts with HIP1,
CC       HIP1 being strongly associated with HTT (By similarity). However, in
CC       mutant HTT proteins with a long poly-Gln region, interaction between
CC       HTT and HIP1 is inhibited, promoting the interaction between HIP1 and
CC       IFT57, leading to apoptosis (By similarity). Interacts with BFAR (By
CC       similarity). Interacts with TTC25 (By similarity). Interacts with USH1G
CC       (By similarity). {ECO:0000250|UniProtKB:Q8BXG3,
CC       ECO:0000250|UniProtKB:Q9NWB7}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q8BXG3}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000269|PubMed:11916979}. Note=Concentrates within the inner
CC       segment of cilia.
CC   -!- TISSUE SPECIFICITY: In retina, detected in the photoreceptor basal body
CC       and connecting cilium. Most abundant in the inner segment of
CC       photoreceptors (at protein level). {ECO:0000269|PubMed:11916979}.
CC   -!- DOMAIN: The pseudo DED region (pDED) mediates the interaction with
CC       HIP1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IFT57 family. {ECO:0000305}.
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DR   EMBL; BT020674; AAX08691.1; -; mRNA.
DR   EMBL; BC151565; AAI51566.1; -; mRNA.
DR   RefSeq; NP_001098873.1; NM_001105403.1.
DR   AlphaFoldDB; Q5EA95; -.
DR   SMR; Q5EA95; -.
DR   STRING; 9913.ENSBTAP00000007606; -.
DR   PaxDb; Q5EA95; -.
DR   PRIDE; Q5EA95; -.
DR   GeneID; 531436; -.
DR   KEGG; bta:531436; -.
DR   CTD; 55081; -.
DR   eggNOG; KOG0972; Eukaryota.
DR   HOGENOM; CLU_039132_0_0_1; -.
DR   InParanoid; Q5EA95; -.
DR   OrthoDB; 839892at2759; -.
DR   TreeFam; TF106156; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0030992; C:intraciliary transport particle B; ISS:UniProtKB.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR   GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   InterPro; IPR019530; Intra-flagellar_transport_57.
DR   PANTHER; PTHR16011; PTHR16011; 1.
DR   Pfam; PF10498; IFT57; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..429
FT                   /note="Intraflagellar transport protein 57 homolog"
FT                   /id="PRO_0000328883"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..426
FT                   /note="pDED"
FT   COILED          305..369
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   429 AA;  48960 MW;  C83DCD427CA311E2 CRC64;
     MAAAAAVVTP SGLEDEVSRS RGEGAGEMVV ERGPGAAYHM FVVMEDLVEK LKLLRYEENL
     LRKNNLKPPS RHYFALPTNP GEQFYMFCTL AAWLINKAGR PFEQPQEYDD PNAIISNILS
     ELRSFGRTAD FPPSKLKSGY GEHVCYVLDC LAEEALKYIG FTWKRPAYPV EELEEETVAE
     DDAELTLNKV DEEFVEEETD NEENFIDLNV LKAQTYRLDM NESAKQEDIL ESTTDAAEWS
     LEVERVLPQL KVTIRTDNKD WRIHVDQMHQ HKSGIESALK ETKGFLDRLH NEISRTLEKI
     GSREKYINNQ LEHLVQEYRA AQAQLSEARE RYQQGNGGVT ERTRILSEVT EELEKVKQEM
     EEKGSSMTDG APLVKIKQSL TKLKQETVQM DIRIGVVEHT LLQSKLKEKS NMTRDMHATI
     IPESAIGSY