DISP1_DANRE
ID DISP1_DANRE Reviewed; 1464 AA.
AC Q6R5J2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein dispatched homolog 1;
DE AltName: Full=Protein chameleon;
GN Name=disp1; Synonyms=con;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=15110707; DOI=10.1016/j.ydbio.2004.01.022;
RA Nakano Y., Kim H.R., Kawakami A., Roy S., Schier A.F., Ingham P.W.;
RT "Inactivation of dispatched 1 by the chameleon mutation disrupts hedgehog
RT signalling in the zebrafish embryo.";
RL Dev. Biol. 269:381-392(2004).
CC -!- FUNCTION: Functions in hedgehog (Hh) signaling. Regulates the release
CC and extracellular accumulation of cholesterol-modified hedgehog
CC proteins and is hence required for effective production of the Hh
CC signal (PubMed:15110707). Synergizes with SCUBE2 to cause an increase
CC in SHH secretion (By similarity). {ECO:0000250|UniProtKB:Q3TDN0,
CC ECO:0000269|PubMed:15110707}.
CC -!- SUBUNIT: Interacts with SHH; via the cholesterol anchor of the dually
CC lipid-modified SHH (ShhNp). {ECO:0000250|UniProtKB:Q3TDN0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout the embryo from
CC fertilization onward. Accumulates at higher levels in the notochord,
CC the ventral floor of the brain as well as dorsal and ventral margins of
CC the myotome. {ECO:0000269|PubMed:15110707}.
CC -!- SIMILARITY: Belongs to the dispatched family. {ECO:0000305}.
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DR EMBL; AY512779; AAR99503.1; -; mRNA.
DR RefSeq; NP_997965.1; NM_212800.1.
DR AlphaFoldDB; Q6R5J2; -.
DR SMR; Q6R5J2; -.
DR STRING; 7955.ENSDARP00000068639; -.
DR PaxDb; Q6R5J2; -.
DR PRIDE; Q6R5J2; -.
DR GeneID; 619201; -.
DR KEGG; dre:619201; -.
DR CTD; 84976; -.
DR ZFIN; ZDB-GENE-030911-7; disp1.
DR eggNOG; KOG3664; Eukaryota.
DR InParanoid; Q6R5J2; -.
DR PhylomeDB; Q6R5J2; -.
DR SignaLink; Q6R5J2; -.
DR PRO; PR:Q6R5J2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0021984; P:adenohypophysis development; IMP:ZFIN.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:ZFIN.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
DR GO; GO:0008015; P:blood circulation; IMP:ZFIN.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0048839; P:inner ear development; IMP:ZFIN.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:ZFIN.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:ZFIN.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF02460; Patched; 2.
DR PROSITE; PS50156; SSD; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1464
FT /note="Protein dispatched homolog 1"
FT /id="PRO_0000310695"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1022..1042
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1065..1085
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 468..640
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1464 AA; 164535 MW; DBFF4B1849702DFD CRC64;
MALSEDFTEL QTLSNGRSSS IFPTTNTPVD PEEEEEQSVS ACTQPNEHTQ MMQTGQNGGL
KSTRLSSSSS SSSQLTDAQR LAVLLPNALP PGFCVCCSLC CNGNQQDCAL FQSAVPSAAL
HMGSCCVQGV PCFCMQHHWP EHLQNQPNMA TLSPPRPFRF PKNYAELIAD WPVVVLGICT
VLIVVCALVG ILVPDLPDFS NPLQGFEPRG TAIGQRLVTW NNMVKNTGYK ATLANYPFKY
ADEQAKSHQD DRWSKDHYDR KKRQAEWDFS KDSFFCDVPG DSYSRIVFAS AEGKNLWNIQ
AIKSMCNFDN TRVRSHPQYL DLCQRTTAAS CCPSWTLGNY IAVLTNKSSC QKITERDVSH
TLNILRSCAK FYHNGTLGPE CWDMTTRKKD LKCGNLPRKC TKYNAVYQIF HFLVDKDFLN
PKNTDYLPPN LKYSMLFAPT EKGETMMNIY LDNFENRNSS DGITTITGIE FGIKHSLFQD
YLLTDTMYPA IAIVIVLVVM CVYTRSMFIT LMTMFAIISS LIVSYFLYRV VFNFDFFPFM
NLTALIILVG IGADDAFVLC DVWNYTKFDK PNSELSETVS ITLQHAALSM FVTSFTTAAA
FYANYVSNIT AIRCFGVYAG TAILVNYILM VTWLPAVVVL HERYLVNLLT CSRTQNHQSQ
GAATFWTSLC QVVNKCLFSI SEASRIFFEK VLPCVVIKLR YLWLLWFLAL TVGGAYVVCV
NPKMKLPSLE LSEFQVFRSS HPFERYDAEY KKLFMFERVN HGEDLHMPIT IIWGVTPIDS
GDPLNPKNKG KLTLDTTFNI ASPASQVWIL NFCQKLRNQS FVYQSEEQDF TSCFMETFKQ
WMENQDCEEA SVYPCCSQST FPYRQDVFEL CIKRAIMELD RSTIYHLDSK TPGPRFDIND
TIRAIVLEFQ STYHFTLAYE KMHQFYREVD TWIQEELRDA PEGLSYGWFV SNLEFYDLQD
SLSDGTLIAM ALSVVVAFSV MLLTTWNIII SLYAIISIAG TIFVTVGSLV LLGWELNVLE
SVTISVAVGL SVDFAVHYGV AYRLAPEPDR EGKVVFSLSR MGSAIAMAAL TTFVAGAMMM
PSTVLAYTQL GTFLMLIMCI SWAFATFFFQ CMCRLLGPQG TCGQIPLPKK LQCAERTSEN
QSTVNNQGKA GACYTTKHEH YELEPLAANV RNEGKASDEE QEACTQLQNN ITSLHDDATL
CASHEEPKHE FENGVQATEH SHLHQYAFNT RCTCENSMHQ YIRERQRTAC HPCGQSRETQ
CATKQSNHLP VCLNRDMIHA PTNSGHFQHC TPSQISRPAA HRCFSGGCGM HAVHISQQQT
ETESYISACV PSSSPQESQN RPAHLQFPDV QRCSSPDTTG VCTLNHDTQN AGELAINSQS
PQKIPWNHLK TKANGTCVLQ DCREVVPEDS IGCRVDKEKT VSPKKFNCFK KNVNAKCNSV
EFHKTRTSVP TIAINSKASS ESLC
