DISP1_HUMAN
ID DISP1_HUMAN Reviewed; 1524 AA.
AC Q96F81; Q8N7C2; Q96I92; Q9H698; Q9H8H9; Q9UFA2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein dispatched homolog 1;
GN Name=DISP1; Synonyms=DISPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Muscle;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-512 AND 596-1524.
RC TISSUE=Kidney epithelium, Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 768-1524.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP FUNCTION, AND INTERACTION WITH SHH.
RX PubMed=22902404; DOI=10.1016/j.celrep.2012.07.010;
RA Tukachinsky H., Kuzmickas R.P., Jao C.Y., Liu J., Salic A.;
RT "Dispatched and scube mediate the efficient secretion of the cholesterol-
RT modified hedgehog ligand.";
RL Cell Rep. 2:308-320(2012).
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 (By similarity). Synergizes with SCUBE2 to cause an increase in
CC SHH secretion (PubMed:22902404). {ECO:0000250|UniProtKB:Q3TDN0,
CC ECO:0000269|PubMed:22902404}.
CC -!- SUBUNIT: Interacts with SHH via the cholesterol anchor of the dually
CC lipid-modified SHH (ShhNp) (PubMed:22902404).
CC {ECO:0000269|PubMed:22902404}.
CC -!- INTERACTION:
CC Q96F81; Q13571: LAPTM5; NbExp=3; IntAct=EBI-10230179, EBI-2865663;
CC Q96F81; O76024: WFS1; NbExp=3; IntAct=EBI-10230179, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dispatched family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07734.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB14637.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15365.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC007734; AAH07734.1; ALT_SEQ; mRNA.
DR EMBL; BC011542; AAH11542.2; -; mRNA.
DR EMBL; AK023679; BAB14637.1; ALT_FRAME; mRNA.
DR EMBL; AK026114; BAB15365.1; ALT_INIT; mRNA.
DR EMBL; AK098669; BAC05373.1; -; mRNA.
DR EMBL; AL133092; CAB61406.1; -; mRNA.
DR CCDS; CCDS1536.1; -.
DR PIR; T42693; T42693.
DR RefSeq; NP_116279.2; NM_032890.3.
DR RefSeq; XP_005273392.1; XM_005273335.2.
DR RefSeq; XP_006711655.1; XM_006711592.2.
DR RefSeq; XP_011508374.1; XM_011510072.2.
DR RefSeq; XP_011508375.1; XM_011510073.2.
DR RefSeq; XP_011508376.1; XM_011510074.2.
DR RefSeq; XP_011508377.1; XM_011510075.2.
DR RefSeq; XP_011508379.1; XM_011510077.2.
DR RefSeq; XP_016858100.1; XM_017002611.1.
DR PDB; 6XE6; EM; 4.54 A; A=172-1249.
DR PDB; 7E2G; EM; 3.61 A; D=1-262, D=281-1524.
DR PDB; 7E2H; EM; 3.68 A; D=1-262, E=281-1524.
DR PDB; 7E2I; EM; 4.07 A; D=1-1524.
DR PDBsum; 6XE6; -.
DR PDBsum; 7E2G; -.
DR PDBsum; 7E2H; -.
DR PDBsum; 7E2I; -.
DR AlphaFoldDB; Q96F81; -.
DR SMR; Q96F81; -.
DR BioGRID; 124405; 15.
DR IntAct; Q96F81; 5.
DR STRING; 9606.ENSP00000284476; -.
DR GlyGen; Q96F81; 2 sites.
DR iPTMnet; Q96F81; -.
DR PhosphoSitePlus; Q96F81; -.
DR BioMuta; DISP1; -.
DR DMDM; 160380707; -.
DR EPD; Q96F81; -.
DR jPOST; Q96F81; -.
DR MassIVE; Q96F81; -.
DR MaxQB; Q96F81; -.
DR PaxDb; Q96F81; -.
DR PeptideAtlas; Q96F81; -.
DR PRIDE; Q96F81; -.
DR ProteomicsDB; 76499; -.
DR Antibodypedia; 34633; 148 antibodies from 32 providers.
DR DNASU; 84976; -.
DR Ensembl; ENST00000284476.7; ENSP00000284476.6; ENSG00000154309.9.
DR Ensembl; ENST00000675039.1; ENSP00000501574.1; ENSG00000154309.9.
DR Ensembl; ENST00000675850.1; ENSP00000502357.1; ENSG00000154309.9.
DR Ensembl; ENST00000675961.1; ENSP00000501808.1; ENSG00000154309.9.
DR GeneID; 84976; -.
DR KEGG; hsa:84976; -.
DR MANE-Select; ENST00000675850.1; ENSP00000502357.1; NM_001377229.1; NP_001364158.1.
DR UCSC; uc057prm.1; human.
DR CTD; 84976; -.
DR DisGeNET; 84976; -.
DR GeneCards; DISP1; -.
DR GeneReviews; DISP1; -.
DR HGNC; HGNC:19711; DISP1.
DR HPA; ENSG00000154309; Low tissue specificity.
DR MalaCards; DISP1; -.
DR MIM; 607502; gene.
DR neXtProt; NX_Q96F81; -.
DR OpenTargets; ENSG00000154309; -.
DR Orphanet; 93925; Alobar holoprosencephaly.
DR Orphanet; 93924; Lobar holoprosencephaly.
DR Orphanet; 280200; Microform holoprosencephaly.
DR Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR Orphanet; 220386; Semilobar holoprosencephaly.
DR Orphanet; 280195; Septopreoptic holoprosencephaly.
DR PharmGKB; PA134938043; -.
DR VEuPathDB; HostDB:ENSG00000154309; -.
DR eggNOG; KOG3664; Eukaryota.
DR GeneTree; ENSGT00940000157407; -.
DR HOGENOM; CLU_004076_1_0_1; -.
DR InParanoid; Q96F81; -.
DR OMA; VYQAACC; -.
DR OrthoDB; 1156918at2759; -.
DR PhylomeDB; Q96F81; -.
DR TreeFam; TF324144; -.
DR PathwayCommons; Q96F81; -.
DR SignaLink; Q96F81; -.
DR SIGNOR; Q96F81; -.
DR BioGRID-ORCS; 84976; 7 hits in 1071 CRISPR screens.
DR ChiTaRS; DISP1; human.
DR GenomeRNAi; 84976; -.
DR Pharos; Q96F81; Tbio.
DR PRO; PR:Q96F81; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96F81; protein.
DR Bgee; ENSG00000154309; Expressed in right testis and 149 other tissues.
DR ExpressionAtlas; Q96F81; baseline and differential.
DR Genevisible; Q96F81; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0060539; P:diaphragm development; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0007225; P:patched ligand maturation; IEA:Ensembl.
DR GO; GO:0015833; P:peptide transport; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1524
FT /note="Protein dispatched homolog 1"
FT /id="PRO_0000310693"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1107..1127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 486..658
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 103
FT /note="E -> K (in dbSNP:rs2609383)"
FT /id="VAR_037077"
FT CONFLICT 195
FT /note="M -> I (in Ref. 2; BAC05373)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="A -> T (in Ref. 3; CAB61406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1379
FT /note="R -> G (in Ref. 2; BAB14637)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="S -> V (in Ref. 2; BAB14637)"
FT /evidence="ECO:0000305"
FT CONFLICT 1408
FT /note="D -> N (in Ref. 1; AAH11542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1524 AA; 170934 MW; 76399E8100DBC648 CRC64;
MAMSNGNNDF VVLSNSSIAT SAANPSPLTP CDGDHAAQQL TPKEATRTKV SPNGCLQLNG
TVKSSFLPLD NQRMPQMLPQ CCHPCPYHHP LTSHSSHQEC HPEAGPAAPS ALASCCMQPH
SEYSASLCPN HSPVYQTTCC LQPSPSFCLH HPWPDHFQHQ PVQQHIANIR PSRPFKLPKS
YAALIADWPV VVLGMCTMFI VVCALVGVLV PELPDFSDPL LGFEPRGTAI GQRLVTWNNM
VKNTGYKATL ANYPFKYADE QAKSHRDDRW SDDHYEREKR EVDWNFHKDS FFCDVPSDRY
SRVVFTSSGG ETLWNLPAIK SMCNVDNSRI RSHPQFGDLC QRTTAASCCP SWTLGNYIAI
LNNRSSCQKI VERDVSHTLK LLRTCAKHYQ NGTLGPDCWD MAARRKDQLK CTNVPRKCTK
YNAVYQILHY LVDKDFMTPK TADYATPALK YSMLFSPTEK GESMMNIYLD NFENWNSSDG
VTTITGIEFG IKHSLFQDYL LMDTVYPAIA IVIVLLVMCV YTKSMFITLM TMFAIISSLI
VSYFLYRVVF HFEFFPFMNL TALIILVGIG ADDAFVLCDV WNYTKFDKPH AETSETVSIT
LQHAALSMFV TSFTTAAAFY ANYVSNITAI RCFGVYAGTA ILVNYVLMVT WLPAVVVLHE
RYLLNIFTCF KKPQQQIYDN KSCWTVACQK CHKVLFAISE ASRIFFEKVL PCIVIKFRYL
WLFWFLALTV GGAYIVCINP KMKLPSLELS EFQVFRSSHP FERYDAEYKK LFMFERVHHG
EELHMPITVI WGVSPEDNGN PLNPKSKGKL TLDSSFNIAS PASQAWILHF CQKLRNQTFF
YQTDEQDFTS CFIETFKQWM ENQDCDEPAL YPCCSHWSFP YKQEIFELCI KRAIMELERS
TGYHLDSKTP GPRFDINDTI RAVVLEFQST YLFTLAYEKM HQFYKEVDSW ISSELSSAPE
GLSNGWFVSN LEFYDLQDSL SDGTLIAMGL SVAVAFSVML LTTWNIIISL YAIISIAGTI
FVTVGSLVLL GWELNVLESV TISVAVGLSV DFAVHYGVAY RLAPDPDREG KVIFSLSRVG
SAMAMAALTT FVAGAMMMPS TVLAYTQLGT FMMLIMCISW AFATFFFQCM CRCLGPQGTC
GQIPLPKKLQ CSAFSHALST SPSDKGQSKT HTINAYHLDP RGPKSELEHE FYELEPLASH
SCTAPEKTTY EETHICSEFF NSQAKNLGMP VHAAYNSELS KSTESDAGSA LLQPPLEQHT
VCHFFSLNQR CSCPDAYKHL NYGPHSCQQM GDCLCHQCSP TTSSFVQIQN GVAPLKATHQ
AVEGFVHPIT HIHHCPCLQG RVKPAGMQNS LPRNFFLHPV QHIQAQEKIG KTNVHSLQRS
IEEHLPKMAE PSSFVCRSTG SLLKTCCDPE NKQRELCKNR DVSNLESSGG TENKAGGKVE
LSLSQTDASV NSEHFNQNEP KVLFNHLMGE AGCRSCPNNS QSCGRIVRVK CNSVDCQMPN
MEANVPAVLT HSELSGESLL IKTL
