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 24-JAN-2024, entry version 148. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-22144; -. DR EMDB; EMD-30956; -. DR EMDB; EMD-30957; -. DR EMDB; EMD-30958; -. DR SMR; Q96F81; -. DR BioGRID; 124405; 16. DR IntAct; Q96F81; 4. DR STRING; 9606.ENSP00000284476; -. DR GlyCosmos; Q96F81; 2 sites, No reported glycans. 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; 9606-ENSP00000284476; -. DR PeptideAtlas; Q96F81; -. DR ProteomicsDB; 76499; -. DR Antibodypedia; 34633; 169 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 AGR; HGNC:19711; -. 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; NGLLAMC; -. DR OrthoDB; 2875706at2759; -. DR PhylomeDB; Q96F81; -. DR TreeFam; TF324144; -. DR PathwayCommons; Q96F81; -. DR SignaLink; Q96F81; -. DR SIGNOR; Q96F81; -. DR BioGRID-ORCS; 84976; 7 hits in 1148 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 male germ line stem cell (sensu Vertebrata) in testis and 151 other cell types or tissues. DR ExpressionAtlas; Q96F81; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:1904680; F:peptide transmembrane transporter activity; ISS:UniProtKB. 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 Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR003392; Ptc/Disp. DR InterPro; IPR000731; SSD. DR PANTHER; PTHR45951:SF4; PROTEIN DISPATCHED HOMOLOG 1; 1. DR PANTHER; PTHR45951; PROTEIN DISPATCHED-RELATED; 1. DR Pfam; PF02460; Patched; 2. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. DR PROSITE; PS50156; SSD; 1. DR Genevisible; Q96F81; HS. 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 //