ID HHAT_HUMAN Reviewed; 493 AA. AC Q5VTY9; B7Z4D5; B7Z5I1; B7Z868; B7ZA75; D3DT91; F5H444; Q17RZ7; Q4G0K3; AC Q5CZ95; Q5TGI2; Q9NVH9; Q9Y3N8; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 10-FEB-2021, entry version 148. DE RecName: Full=Protein-cysteine N-palmitoyltransferase HHAT; DE EC=2.3.1.-; DE AltName: Full=Hedgehog acyltransferase; DE AltName: Full=Melanoma antigen recognized by T-cells 2; DE Short=MART-2; DE AltName: Full=Skinny hedgehog protein 1; GN Name=HHAT; Synonyms=MART2, SKI1; 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 [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, RP GTP-BINDING, CHARACTERIZATION OF VARIANT GLU-448, AND VARIANT SER-450. RC TISSUE=Melanoma; RX PubMed=11160356; DOI=10.4049/jimmunol.166.4.2871; RA Kawakami Y., Wang X., Shofuda T., Sumimoto H., Tupesis J., Fitzgerald E., RA Rosenberg S.; RT "Isolation of a new melanoma antigen, MART-2, containing a mutated epitope RT recognized by autologous tumor-infiltrating T lymphocytes."; RL J. Immunol. 166:2871-2877(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5; 6 AND 7), AND RP VARIANT ARG-188. RC TISSUE=Brain, Lung, Teratocarcinoma, Testis, and Trachea; 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] (ISOFORM 4). RC TISSUE=Brain cortex; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-182. RC TISSUE=Brain, and Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-335 (ISOFORM 2). RA Rhodes S.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 328-390 (ISOFORM 1), AND FUNCTION. RX PubMed=11486055; DOI=10.1126/science.1064437; RA Chamoun Z., Mann R.K., Nellen D., von Kessler D.P., Bellotto M., RA Beachy P.A., Basler K.; RT "Skinny hedgehog, an acyltransferase required for palmitoylation and RT activity of the hedgehog signal."; RL Science 293:2080-2084(2001). RN [9] RP SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=25488661; DOI=10.1074/jbc.m114.625764; RA Matevossian A., Resh M.D.; RT "Membrane topology of hedgehog acyltransferase."; RL J. Biol. Chem. 290:2235-2243(2015). RN [10] RP SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION AT CYS-188; CYS-242; RP CYS-324 AND CYS-410. RX PubMed=25505265; DOI=10.1074/jbc.m114.614578; RA Konitsiotis A.D., Jovanovic B., Ciepla P., Spitaler M., Lanyon-Hogg T., RA Tate E.W., Magee A.I.; RT "Topological analysis of Hedgehog acyltransferase, a multipalmitoylated RT transmembrane protein."; RL J. Biol. Chem. 290:3293-3307(2015). CC -!- FUNCTION: Catalyzes N-terminal palmitoylation of SHH; which is required CC for SHH signaling. May bind GTP. {ECO:0000250, CC ECO:0000269|PubMed:11486055}. CC -!- INTERACTION: CC Q5VTY9; O00560: SDCBP; NbExp=3; IntAct=EBI-12951255, EBI-727004; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:25488661, ECO:0000269|PubMed:25505265}; Multi-pass CC membrane protein {ECO:0000269|PubMed:25488661, CC ECO:0000269|PubMed:25505265}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q5VTY9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VTY9-2; Sequence=VSP_016686, VSP_016689; CC Name=3; CC IsoId=Q5VTY9-3; Sequence=VSP_016689; CC Name=4; CC IsoId=Q5VTY9-4; Sequence=VSP_016685, VSP_016687, VSP_016688; CC Name=5; CC IsoId=Q5VTY9-5; Sequence=VSP_016686; CC Name=6; CC IsoId=Q5VTY9-6; Sequence=VSP_043481; CC Name=7; CC IsoId=Q5VTY9-7; Sequence=VSP_044968; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues and cancer CC cell lines. {ECO:0000269|PubMed:11160356}. CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family. HHAT CC subfamily. {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; AK001586; BAA91772.1; -; mRNA. DR EMBL; AK297193; BAH12521.1; -; mRNA. DR EMBL; AK298991; BAH12917.1; -; mRNA. DR EMBL; AK302955; BAH13854.1; -; mRNA. DR EMBL; AK316190; BAH14561.1; -; mRNA. DR EMBL; AK316524; BAH14895.1; -; mRNA. DR EMBL; CR936628; CAI56771.1; -; mRNA. DR EMBL; AC096636; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL034351; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035414; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590653; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL691441; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX255872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93427.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93428.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93430.1; -; Genomic_DNA. DR EMBL; BC117130; AAI17131.1; -; mRNA. DR EMBL; AL049848; CAB42852.1; -; mRNA. DR CCDS; CCDS1495.1; -. [Q5VTY9-1] DR CCDS; CCDS53471.1; -. [Q5VTY9-7] DR CCDS; CCDS53472.1; -. [Q5VTY9-5] DR CCDS; CCDS53473.1; -. [Q5VTY9-6] DR RefSeq; NP_001116306.1; NM_001122834.3. [Q5VTY9-1] DR RefSeq; NP_001164035.1; NM_001170564.2. [Q5VTY9-6] DR RefSeq; NP_001164051.1; NM_001170580.2. [Q5VTY9-1] DR RefSeq; NP_001164058.1; NM_001170587.2. [Q5VTY9-7] DR RefSeq; NP_001164059.1; NM_001170588.2. [Q5VTY9-5] DR RefSeq; NP_060664.2; NM_018194.5. [Q5VTY9-1] DR RefSeq; XP_011508041.1; XM_011509739.2. [Q5VTY9-3] DR RefSeq; XP_011508042.1; XM_011509740.2. [Q5VTY9-3] DR RefSeq; XP_011508043.1; XM_011509741.2. [Q5VTY9-3] DR RefSeq; XP_011508048.1; XM_011509746.2. [Q5VTY9-2] DR RefSeq; XP_016857218.1; XM_017001729.1. [Q5VTY9-3] DR RefSeq; XP_016857221.1; XM_017001732.1. [Q5VTY9-5] DR RefSeq; XP_016857224.1; XM_017001735.1. [Q5VTY9-5] DR RefSeq; XP_016857226.1; XM_017001737.1. [Q5VTY9-6] DR PDB; 6P64; X-ray; 3.05 A; C/H=68-76. DR PDB; 6UJO; X-ray; 2.25 A; C=68-76. DR PDB; 6UJQ; X-ray; 2.55 A; C=68-76. DR PDB; 6UK2; X-ray; 3.14 A; C=68-76. DR PDB; 6UK4; X-ray; 2.70 A; C=68-76. DR PDBsum; 6P64; -. DR PDBsum; 6UJO; -. DR PDBsum; 6UJQ; -. DR PDBsum; 6UK2; -. DR PDBsum; 6UK4; -. DR SMR; Q5VTY9; -. DR BioGRID; 120852; 1. DR IntAct; Q5VTY9; 1. DR STRING; 9606.ENSP00000438468; -. DR SwissLipids; SLP:000001949; -. DR TCDB; 2.A.50.1.4; the glycerol uptake (gup) or membrane-bound acyl transfeerase (mboat) family. DR iPTMnet; Q5VTY9; -. DR PhosphoSitePlus; Q5VTY9; -. DR SwissPalm; Q5VTY9; -. DR BioMuta; HHAT; -. DR DMDM; 74747010; -. DR jPOST; Q5VTY9; -. DR MassIVE; Q5VTY9; -. DR PaxDb; Q5VTY9; -. DR PeptideAtlas; Q5VTY9; -. DR PRIDE; Q5VTY9; -. DR ProteomicsDB; 26462; -. DR ProteomicsDB; 65361; -. [Q5VTY9-1] DR ProteomicsDB; 65362; -. [Q5VTY9-2] DR ProteomicsDB; 65363; -. [Q5VTY9-3] DR ProteomicsDB; 65364; -. [Q5VTY9-4] DR ProteomicsDB; 65365; -. [Q5VTY9-5] DR ProteomicsDB; 65366; -. [Q5VTY9-6] DR Antibodypedia; 47111; 113 antibodies. DR DNASU; 55733; -. DR Ensembl; ENST00000261458; ENSP00000261458; ENSG00000054392. [Q5VTY9-1] DR Ensembl; ENST00000367010; ENSP00000355977; ENSG00000054392. [Q5VTY9-1] DR Ensembl; ENST00000413764; ENSP00000416845; ENSG00000054392. [Q5VTY9-1] DR Ensembl; ENST00000537898; ENSP00000442625; ENSG00000054392. [Q5VTY9-5] DR Ensembl; ENST00000541565; ENSP00000444995; ENSG00000054392. [Q5VTY9-6] DR Ensembl; ENST00000545154; ENSP00000438468; ENSG00000054392. [Q5VTY9-7] DR Ensembl; ENST00000625523; ENSP00000486634; ENSG00000280680. [Q5VTY9-6] DR Ensembl; ENST00000625820; ENSP00000486054; ENSG00000280680. [Q5VTY9-1] DR Ensembl; ENST00000626327; ENSP00000487414; ENSG00000280680. [Q5VTY9-5] DR Ensembl; ENST00000627903; ENSP00000487400; ENSG00000280680. [Q5VTY9-1] DR Ensembl; ENST00000628693; ENSP00000486611; ENSG00000280680. [Q5VTY9-7] DR Ensembl; ENST00000629360; ENSP00000486128; ENSG00000280680. [Q5VTY9-1] DR GeneID; 55733; -. DR KEGG; hsa:55733; -. DR UCSC; uc001hhz.5; human. [Q5VTY9-1] DR CTD; 55733; -. DR DisGeNET; 55733; -. DR GeneCards; HHAT; -. DR HGNC; HGNC:18270; HHAT. DR HPA; ENSG00000054392; Low tissue specificity. DR MalaCards; HHAT; -. DR MIM; 605743; gene. DR neXtProt; NX_Q5VTY9; -. DR OpenTargets; ENSG00000054392; -. DR Orphanet; 1422; Chondrodysplasia-disorder of sex development syndrome. DR PharmGKB; PA134926499; -. DR VEuPathDB; HostDB:ENSG00000054392.12; -. DR eggNOG; KOG3860; Eukaryota. DR GeneTree; ENSGT00530000063629; -. DR HOGENOM; CLU_027533_3_1_1; -. DR InParanoid; Q5VTY9; -. DR OMA; IHYMSRD; -. DR OrthoDB; 392243at2759; -. DR PhylomeDB; Q5VTY9; -. DR TreeFam; TF315826; -. DR PathwayCommons; Q5VTY9; -. DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-HSA-5658034; HHAT G278V abrogates palmitoylation of Hh-Np. DR SignaLink; Q5VTY9; -. DR SIGNOR; Q5VTY9; -. DR BioGRID-ORCS; 55733; 4 hits in 871 CRISPR screens. DR ChiTaRS; HHAT; human. DR GenomeRNAi; 55733; -. DR Pharos; Q5VTY9; Tbio. DR PRO; PR:Q5VTY9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5VTY9; protein. DR Bgee; ENSG00000054392; Expressed in right adrenal gland and 168 other tissues. DR ExpressionAtlas; Q5VTY9; baseline and differential. DR Genevisible; Q5VTY9; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0008374; F:O-acyltransferase activity; TAS:Reactome. DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IBA:GO_Central. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl. DR InterPro; IPR032981; HHAT. DR InterPro; IPR004299; MBOAT_fam. DR PANTHER; PTHR13285:SF20; PTHR13285:SF20; 1. DR Pfam; PF03062; MBOAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Alternative splicing; Developmental protein; KW Endoplasmic reticulum; GTP-binding; Lipoprotein; Membrane; KW Nucleotide-binding; Palmitate; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..493 FT /note="Protein-cysteine N-palmitoyltransferase HHAT" FT /id="PRO_0000213134" FT TOPO_DOM 1..5 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 6..22 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 23..67 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 68..84 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 85..94 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 95..119 FT /evidence="ECO:0000255" FT TOPO_DOM 120..131 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 132..148 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 149..162 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 163..183 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 184..202 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 203..217 FT /evidence="ECO:0000255" FT TOPO_DOM 218..243 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 244..271 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 272..281 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 282..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 311..363 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 364..380 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 381..383 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 384..399 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 400..427 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 428..448 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 449..462 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 463..481 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 482..493 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 448..455 FT /note="GTP-binding" FT /evidence="ECO:0000305|PubMed:11160356" FT ACT_SITE 379 FT /evidence="ECO:0000255" FT LIPID 188 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:25505265" FT LIPID 242 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:25505265" FT LIPID 324 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:25505265" FT LIPID 410 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:25505265" FT VAR_SEQ 1..369 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_016685" FT VAR_SEQ 1..30 FT /note="MLPRWELALYLLASLGFHFYSFYEVYKVSR -> MSLGLGSAERGVLGTRGA FT RERCRRRRPGQPG (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044968" FT VAR_SEQ 91..155 FT /note="Missing (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11160356, FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7" FT /id="VSP_016686" FT VAR_SEQ 92..228 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043481" FT VAR_SEQ 416..451 FT /note="ARYFSPQARRRFHAALASCSTSMLILSNLVFLGGNE -> VSRILAPVLGDS FT GTRQIRFIRDGAIRFPAPTMGPFY (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_016687" FT VAR_SEQ 452..493 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_016688" FT VAR_SEQ 465..493 FT /note="WPWVTLSVLGFLYCYSHVGIAWAQTYATD -> GLFLFFLLNPCWETAFQGF FT PVFLHFLQTEVLATFVPNYFSWNICIENTSELSSY (in isoform 2 and FT isoform 3)" FT /evidence="ECO:0000303|PubMed:11160356, ECO:0000303|Ref.7" FT /id="VSP_016689" FT VARIANT 165 FT /note="E -> G (in dbSNP:rs2228898)" FT /id="VAR_050024" FT VARIANT 182 FT /note="S -> N (in dbSNP:rs2294851)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_024743" FT VARIANT 188 FT /note="C -> R (in dbSNP:rs34228541)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_061336" FT VARIANT 448 FT /note="G -> E (in a melanoma cell line; abolishes GTP- FT binding; dbSNP:rs757163023)" FT /evidence="ECO:0000269|PubMed:11160356" FT /id="VAR_024744" FT VARIANT 450 FT /note="N -> S (in a lung cancer cell line; FT dbSNP:rs147954610)" FT /evidence="ECO:0000269|PubMed:11160356" FT /id="VAR_024745" FT CONFLICT 2 FT /note="L -> P (in Ref. 2; BAA91772)" FT /evidence="ECO:0000305" FT CONFLICT 204 FT /note="M -> V (in Ref. 2; BAH14561)" FT /evidence="ECO:0000305" FT CONFLICT 450 FT /note="N -> D (in Ref. 2; BAA91772)" FT /evidence="ECO:0000305" SQ SEQUENCE 493 AA; 57313 MW; 5E962E2A61F2DE15 CRC64; MLPRWELALY LLASLGFHFY SFYEVYKVSR EHEEELDQEF ELETDTLFGG LKKDATDFEW SFWMEWGKQW LVWLLLGHMV VSQMATLLAR KHRPWILMLY GMWACWCVLG TPGVAMVLLH TTISFCVAQF RSQLLTWLCS LLLLSTLRLQ GVEEVKRRWY KTENEYYLLQ FTLTVRCLYY TSFSLELCWQ QLPAASTSYS FPWMLAYVFY YPVLHNGPIL SFSEFIKQMQ QQEHDSLKAS LCVLALGLGR LLCWWWLAEL MAHLMYMHAI YSSIPLLETV SCWTLGGLAL AQVLFFYVKY LVLFGVPALL MRLDGLTPPA LPRCVSTMFS FTGMWRYFDV GLHNFLIRYV YIPVGGSQHG LLGTLFSTAM TFAFVSYWHG GYDYLWCWAA LNWLGVTVEN GVRRLVETPC IQDSLARYFS PQARRRFHAA LASCSTSMLI LSNLVFLGGN EVGKTYWNRI FIQGWPWVTL SVLGFLYCYS HVGIAWAQTY ATD //