DISP3_CHICK
ID DISP3_CHICK Reviewed; 1338 AA.
AC B9U3F2; F1NH44;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein dispatched homolog 3 {ECO:0000250|UniProtKB:Q9P2K9};
DE AltName: Full=Patched domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Thyroid hormone receptor up-regulated protein 1 {ECO:0000303|PubMed:19179482};
DE Short=TRUP1 {ECO:0000303|PubMed:19179482};
GN Name=DISP3 {ECO:0000250|UniProtKB:Q9P2K9}; Synonyms=PTCHD2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:ACB78184.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Erythroid cell;
RX PubMed=19179482; DOI=10.1210/me.2008-0271;
RA Zikova M., Corlett A., Bendova Z., Pajer P., Bartunek P.;
RT "DISP3, a sterol-sensing domain-containing protein that links thyroid
RT hormone action and cholesterol metabolism.";
RL Mol. Endocrinol. 23:520-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Plays a role in neuronal proliferation and differentiation
CC (By similarity). Plays a role in the accumulation of cellular
CC cholesterol (PubMed:19179482). Involved in intracellular lipid droplet
CC formation (PubMed:19179482). May contribute to cholesterol homeostasis
CC in neuronal cells (PubMed:19179482). {ECO:0000250|UniProtKB:Q9P2K9,
CC ECO:0000269|PubMed:19179482}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein
CC {ECO:0000305}. Nucleus membrane {ECO:0000269|PubMed:19179482}; Multi-
CC pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:19179482}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Predominantly localized to cholesterol-enriched
CC domains within membranes (PubMed:19179482). Localizes to cytoplasmic
CC punctate vesicular structures (PubMed:19179482).
CC {ECO:0000269|PubMed:19179482}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, hippocampus and cerebellum
CC (PubMed:19179482). Expressed in the ganglion and bipolar cells of the
CC inner and outer nuclear layers of the retina and in Purkinje cells (at
CC protein level) (PubMed:19179482). Expressed strongly in brain and
CC retina, weakly in testis and bone marrow (PubMed:19179482).
CC {ECO:0000269|PubMed:19179482}.
CC -!- INDUCTION: Down-regulated by thyroid hormone T3 in retinal ganglion
CC layers during the embryonic development (PubMed:19179482).
CC {ECO:0000269|PubMed:19179482}.
CC -!- DOMAIN: The SSD (sterol-sensing) domain is necessary for the increase
CC in cellular cholesterol uptake (PubMed:19179482).
CC {ECO:0000269|PubMed:19179482}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; EU429800; ACB78184.1; -; mRNA.
DR EMBL; AADN03008029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001186105.1; NM_001199176.1.
DR RefSeq; XP_015152410.1; XM_015296924.1.
DR RefSeq; XP_015152411.1; XM_015296925.1.
DR RefSeq; XP_015152412.1; XM_015296926.1.
DR RefSeq; XP_015152413.1; XM_015296927.1.
DR RefSeq; XP_015152414.1; XM_015296928.1.
DR AlphaFoldDB; B9U3F2; -.
DR STRING; 9031.ENSGALP00000007415; -.
DR PaxDb; B9U3F2; -.
DR Ensembl; ENSGALT00000007427; ENSGALP00000007415; ENSGALG00000004662.
DR GeneID; 419497; -.
DR KEGG; gga:419497; -.
DR CTD; 57540; -.
DR VEuPathDB; HostDB:geneid_419497; -.
DR eggNOG; KOG3664; Eukaryota.
DR GeneTree; ENSGT00940000157931; -.
DR HOGENOM; CLU_007038_0_0_1; -.
DR OMA; WDYSRTY; -.
DR OrthoDB; 56949at2759; -.
DR PhylomeDB; B9U3F2; -.
DR TreeFam; TF331579; -.
DR PRO; PR:B9U3F2; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000004662; Expressed in cerebellum and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IEP:UniProtKB.
DR InterPro; IPR042480; DISP3.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR46687; PTHR46687; 2.
DR Pfam; PF02460; Patched; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Cholesterol metabolism; Cytoplasmic vesicle; Differentiation;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Nucleus;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1338
FT /note="Protein dispatched homolog 3"
FT /id="PRO_0000436016"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..406
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..452
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..1128
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 1129..1149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1172..1237
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1267..1287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1288..1302
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1324..1338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 401..559
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 164..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 148330 MW; 686B98D488787BA9 CRC64;
MDTEDDPLLQ DAWLDEEDEE VAFSSRKRRE GALLCGKSSC RVRPLRVTLP VSGFWNIVGW
IFTNPYCAGF ILFLGCAIPA VLAVVMFLHY PALDIDISYN AFEIRNHESS QRFDALALAL
KSQFGSWGRN RRDLADFTSE TLQRLIFEQL QQLHLNASHL QVSTRAKRSA PQGRTSSPEP
RAHPHPGNET SRVTRGAPRW DYSNTYISAN TQTHAHWRIE LIFLARGDSE NNIFTTERLV
TIHEVERKIM DHPRFREFCW KPHEVLKDLP LGSYSYCSPP SSLMTYFFPT ERGGKIYYDG
MGQDLADIQG SLELAMTHPE FYWYVDEGLS AENKKSSLLR SEILFGAPLP NYYSVEDRWE
EQRHKFQNFV VTYVAMLAKQ STSKVQVLYG GTDLFDYEVR RTFNNDMLLA FISSSCIAVL
VYILTSCSVF LSFFGIASIG LSCLVALFLY HVVFGIQYLG ILNGVAAFVI VGIGVDDVFV
FINTYRQATH LKDLRLRMIH TIQTAGKATF FTSLTTAAAY AANIFSQIPA VHDFGLFMSL
IVSCCWVAVL FTMPAALGIW TLYVSPLESS CQNSCSQKCT KKSTLHLAED LFVASEGTSR
AGRETLPYLD DDIPLLSVEE EPVSLEMGDV PLVSVMPENL QLPVEKSNRG HLIAHLQELL
EHWVLWSAVK SRWVIVGLFL LVLLLSIFFA SRLRPASRAP VLFRPDTNIQ VLLDLKYNLS
AEGISCITCS GLFQEKPHSL QNNFRTSLEK KKRGSASPWG SKGSISDTGQ QDLQGTVYIS
KSRSKGRPAI YRFSLNASIP APWQMVSPGD GEVPSFQVYR VPFGNFTRKL TACVSTVGLL
KQTSPRKWMM TTLSCDSKRG WKFDFSFYVA AKEQQRTRKL YFAQSHKPPY HGRVCVAPPG
CLLSSSPDGP TKGILYVPSE KAAPKARLSA TSGFNPCMNM GCGKPAVRPL VDTGAMVFVV
FGIRGVNRTK NSDNHVIGDM GSVIYDDSFD LFKEIGNLCR LCKAIASNTE LVKPGGAQCL
PSGYSISSFL QMLHPECKNI PEPNLLPGQL SHGAVGVKDG KVQWISMAFE STTYKGKSSF
QTYADYLKWE TFLQQQLQLF PEGSALRHGF QTCEHWKQIF MEIIGVQSAL YGLILSLVIC
VAAVAVFTTH ILLLLPVLLS ILGVVCLVVT IMYWSGWEMG AVEAISLSIL VGSSVDYCVH
LVEGYLLAGE NLPLHHAEDP TACRQWRTIE AIRHVGVAIV SSAVTTVIAT VPLFFCIIAP
FAKFGKIVAL NTGVSILYTL TVSTALLSIM GPGTFTRSRT SCLKAVAGVL LAGLLGLCIC
LALLKGGFKI PLPNGTAL
