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HighlightsDISP1 is encoded by the DISP1 gene and is also known as Protein dispatched homolog 1 and DISPA. The DISP1 gene is one of two human homologs of Drosophila dispatched, and the encoded protein may play an essential role in hedgehog (HH) patterning activities in the early embryo. DISP1 is a twelve transmembrane domain protein that is required for long-range sonic hedgehog (Shh) signaling. Inhibition of DISP1 function, both by RNAi or dominant-negative constructs, prevents secretion and results in the accumulation of Shh in source cells.
| Basic Information of DISP1 | |
| Protein Name | Protein dispatched homolog 1 |
| Gene Name | DISP1 |
| Aliases | DISPA |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q96F81 |
| Transmembrane Times | 12 |
| Length (aa) | 1524 |
| Sequence | MAMSNGNNDFVVLSNSSIATSAANPSPLTPCDGDHAAQQLTPKEATRTKVSPNGCLQLNGTVKSSFLPLDNQRMPQMLPQCCHPCPYHHPLTSHSSHQECHPEAGPAAPSALASCCMQPHSEYSASLCPNHSPVYQTTCCLQPSPSFCLHHPWPDHFQHQPVQQHIANIRPSRPFKLPKSYAALIADWPVVVLGMCTMFIVVCALVGVLVPELPDFSDPLLGFEPRGTAIGQRLVTWNNMVKNTGYKATLANYPFKYADEQAKSHRDDRWSDDHYEREKREVDWNFHKDSFFCDVPSDRYSRVVFTSSGGETLWNLPAIKSMCNVDNSRIRSHPQFGDLCQRTTAASCCPSWTLGNYIAILNNRSSCQKIVERDVSHTLKLLRTCAKHYQNGTLGPDCWDMAARRKDQLKCTNVPRKCTKYNAVYQILHYLVDKDFMTPKTADYATPALKYSMLFSPTEKGESMMNIYLDNFENWNSSDGVTTITGIEFGIKHSLFQDYLLMDTVYPAIAIVIVLLVMCVYTKSMFITLMTMFAIISSLIVSYFLYRVVFHFEFFPFMNLTALIILVGIGADDAFVLCDVWNYTKFDKPHAETSETVSITLQHAALSMFVTSFTTAAAFYANYVSNITAIRCFGVYAGTAILVNYVLMVTWLPAVVVLHERYLLNIFTCFKKPQQQIYDNKSCWTVACQKCHKVLFAISEASRIFFEKVLPCIVIKFRYLWLFWFLALTVGGAYIVCINPKMKLPSLELSEFQVFRSSHPFERYDAEYKKLFMFERVHHGEELHMPITVIWGVSPEDNGNPLNPKSKGKLTLDSSFNIASPASQAWILHFCQKLRNQTFFYQTDEQDFTSCFIETFKQWMENQDCDEPALYPCCSHWSFPYKQEIFELCIKRAIMELERSTGYHLDSKTPGPRFDINDTIRAVVLEFQSTYLFTLAYEKMHQFYKEVDSWISSELSSAPEGLSNGWFVSNLEFYDLQDSLSDGTLIAMGLSVAVAFSVMLLTTWNIIISLYAIISIAGTIFVTVGSLVLLGWELNVLESVTISVAVGLSVDFAVHYGVAYRLAPDPDREGKVIFSLSRVGSAMAMAALTTFVAGAMMMPSTVLAYTQLGTFMMLIMCISWAFATFFFQCMCRCLGPQGTCGQIPLPKKLQCSAFSHALSTSPSDKGQSKTHTINAYHLDPRGPKSELEHEFYELEPLASHSCTAPEKTTYEETHICSEFFNSQAKNLGMPVHAAYNSELSKSTESDAGSALLQPPLEQHTVCHFFSLNQRCSCPDAYKHLNYGPHSCQQMGDCLCHQCSPTTSSFVQIQNGVAPLKATHQAVEGFVHPITHIHHCPCLQGRVKPAGMQNSLPRNFFLHPVQHIQAQEKIGKTNVHSLQRSIEEHLPKMAEPSSFVCRSTGSLLKTCCDPENKQRELCKNRDVSNLESSGGTENKAGGKVELSLSQTDASVNSEHFNQNEPKVLFNHLMGEAGCRSCPNNSQSCGRIVRVKCNSVDCQMPNMEANVPAVLTHSELSGESLLIKTL |
The action of DISP1 is required in the Shh signaling pathway. DISP1 shares many characteristics with members of the resistance-nodulation-cell division (RND) family of proton-driven transporters. Not only are the overall structures of Disp1 similar to that of bacterial RND permeases, but aspartic acid residues in the fourth transmembrane span, which are thought to be important for proton translocation, are also conserved. It has previously been shown that bacterial RND permeases function as trimers. Similarly, it has been shown that DISP1 is also assembled into trimers. Similar lysates analyzed on an SDS PAGE gel resolves that DISP1 is located basolaterally in polarized epithelial cells and assembles as trimers. DISP1 is required for the basolateral secretion of Shh and lipid-modified. Meanwhile, Shh secretes in a DISP1-dependent manner and is retained in the extracellular matrix.
Fig.1 The signaling pathway of DISP1 in transporting Shh (Boise, 2014).
The observations in this article support a dual role for DISP1, not only in the secretion of Shh from the source cells but also in the subsequent transport of Shh through tissue.
This article reveals that deletion or variants of DISP1 have been proposed as a candidate for the midline defects in this syndrome but may not be responsible for its major features in some cases. Meanwhile, the results of this article may help define the role of the DISP1 haploinsufficiency in phenotype and support the suggestion that DISP1 mutation or deletion may reveal incomplete penetrance.
The analyses of this article about the Disp1C829F mutation demonstrate that DISP1 is not absolutely required for the paracrine signaling role of Ihh in the skeleton and Disp1 is critical for the full extent of signaling within the chondrocyte target field and consequently the establishment of a normal skeletal growth plate.
Authors in this article perform an extensive mutational analysis of the entire human DISP1 gene, required for secretion of all hedgehog ligand and the data of this article suggest that DISP1 function contributes substantially to both of these signs in humans.
The article investigates the relationship between the DISP1 rs17162912 genotype distribution and serotonin reuptake inhibitor response and there is no observe a significant association between rs17162912 and serotonin reuptake inhibitor response.
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Besides, aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-DISP1 antibody development services.
As a forward-looking research institute as well as a leading custom service provider in the field of membrane protein, Creative Biolabs has extensive experience to offer the novel human or functional membrane proteins services for our worldwide customers. Please feel free to contact us for more information.
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