PGAP6_HUMAN
ID PGAP6_HUMAN Reviewed; 771 AA.
AC Q9HCN3; D3DU49; Q4TT35; Q8WU24; Q96S25; Q9BR03; Q9BT97; Q9H7B9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Post-GPI attachment to proteins factor 6 {ECO:0000303|PubMed:27881714};
DE EC=3.1.1.4 {ECO:0000305|PubMed:27881714};
DE AltName: Full=GPI processing phospholipase A2 {ECO:0000303|PubMed:27881714};
DE Short=GPI-PLA2 {ECO:0000303|PubMed:27881714};
DE AltName: Full=Protein M83;
DE AltName: Full=Transmembrane protein 6;
DE AltName: Full=Transmembrane protein 8;
DE AltName: Full=Transmembrane protein 8A;
DE Flags: Precursor;
GN Name=PGAP6 {ECO:0000303|PubMed:27881714, ECO:0000312|HGNC:HGNC:17205};
GN Synonyms=TMEM6, TMEM8, TMEM8A;
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], TISSUE SPECIFICITY, GLYCOSYLATION, AND VARIANTS
RP VARIANT ALA-136 AND VAL-310.
RX PubMed=11006113; DOI=10.1006/bbrc.2000.3409;
RA Motohashi T., Miyoshi S., Osawa M., Eyre H.J., Sutherland G.R., Matsuda Y.,
RA Nakamura Y., Shibuya A., Iwama A., Nakauchi H.;
RT "Molecular cloning and chromosomal mapping of a novel five-span
RT transmembrane protein gene, M83.";
RL Biochem. Biophys. Res. Commun. 276:244-250(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-136.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-136 AND VAL-310.
RC TISSUE=Pancreas, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-771, AND VARIANTS VAL-310 AND
RP TRP-567.
RC TISSUE=Coronary artery;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21752829; DOI=10.1093/hmg/ddr306;
RA Palmieri M., Impey S., Kang H., di Ronza A., Pelz C., Sardiello M.,
RA Ballabio A.;
RT "Characterization of the CLEAR network reveals an integrated control of
RT cellular clearance pathways.";
RL Hum. Mol. Genet. 20:3852-3866(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-584; HIS-588;
RP ASP-610; HIS-722 AND HIS-726.
RX PubMed=27881714; DOI=10.1083/jcb.201605121;
RA Lee G.H., Fujita M., Takaoka K., Murakami Y., Fujihara Y., Kanzawa N.,
RA Murakami K.I., Kajikawa E., Takada Y., Saito K., Ikawa M., Hamada H.,
RA Maeda Y., Kinoshita T.;
RT "A GPI processing phospholipase A2, PGAP6, modulates Nodal signaling in
RT embryos by shedding CRIPTO.";
RL J. Cell Biol. 215:705-718(2016).
RN [9]
RP FUNCTION.
RX PubMed=27835684; DOI=10.1371/journal.pone.0166715;
RA Castro-Castro A., Muriel O., Del Pozo M.A., Bustelo X.R.;
RT "Characterization of novel molecular mechanisms favoring Rac1 membrane
RT translocation.";
RL PLoS ONE 11:E0166715-E0166715(2016).
RN [10]
RP LACK OF FUSOGENIC ACTIVITY.
RX PubMed=26858401; DOI=10.1073/pnas.1600101113;
RA Millay D.P., Gamage D.G., Quinn M.E., Min Y.L., Mitani Y., Bassel-Duby R.,
RA Olson E.N.;
RT "Structure-function analysis of myomaker domains required for myoblast
RT fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2116-2121(2016).
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Lipid remodeling steps consist in the generation of 2
CC saturated fatty chains at the sn-2 position of GPI-anchor proteins
CC (GPI-AP). Has phospholipase A2 activity that removes an acyl-chain at
CC the sn-2 position of GPI-anchors during the remodeling of GPI. Required
CC for the shedding of the GPI-AP TDGF1, but not CFC1, at the cell
CC surface. Shedding of TDGF1 modulates Nodal signaling by allowing
CC soluble TDGF1 to act as a Nodal coreceptor on other cells
CC (PubMed:27881714). Also indirectly involved in the translocation of
CC RAC1 from the cytosol to the plasma membrane by maintaining the steady
CC state amount of CAV1-enriched plasma membrane subdomains, stabilizing
CC RAC1 at the plasma membrane (PubMed:27835684). In contrast to myomaker
CC (TMEM8C), has no fusogenic activity (PubMed:26858401).
CC {ECO:0000269|PubMed:26858401, ECO:0000269|PubMed:27835684,
CC ECO:0000269|PubMed:27881714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000305|PubMed:27881714};
CC -!- INTERACTION:
CC Q9HCN3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10310808, EBI-3867333;
CC Q9HCN3; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-10310808, EBI-7060731;
CC Q9HCN3; Q15323: KRT31; NbExp=3; IntAct=EBI-10310808, EBI-948001;
CC Q9HCN3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10310808, EBI-11959885;
CC Q9HCN3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10310808, EBI-10172290;
CC Q9HCN3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10310808, EBI-10171774;
CC Q9HCN3; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10310808, EBI-11953334;
CC Q9HCN3; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-10310808, EBI-3958099;
CC Q9HCN3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10310808, EBI-22310682;
CC Q9HCN3; Q04864: REL; NbExp=3; IntAct=EBI-10310808, EBI-307352;
CC Q9HCN3; Q04864-2: REL; NbExp=3; IntAct=EBI-10310808, EBI-10829018;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27881714};
CC Multi-pass membrane protein {ECO:0000255}. Lysosome membrane
CC {ECO:0000269|PubMed:21752829}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, placenta, spleen, liver,
CC kidney, bone marrow, peripheral blood leukocytes and tonsil.
CC {ECO:0000269|PubMed:11006113}.
CC -!- INDUCTION: Repressed during activation of CD4+ and CD8+ T-lymphocytes.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11006113}.
CC -!- SIMILARITY: Belongs to the TMEM8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14975.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB045292; BAB16376.1; -; mRNA.
DR EMBL; AE006463; AAK61227.1; -; Genomic_DNA.
DR EMBL; Z97634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85824.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85825.1; -; Genomic_DNA.
DR EMBL; BC021557; AAH21557.1; -; mRNA.
DR EMBL; BC004276; AAH04276.1; -; mRNA.
DR EMBL; AK024725; BAB14975.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10407.1; -.
DR PIR; JC7388; JC7388.
DR RefSeq; NP_067082.2; NM_021259.2.
DR AlphaFoldDB; Q9HCN3; -.
DR BioGRID; 121856; 29.
DR IntAct; Q9HCN3; 16.
DR STRING; 9606.ENSP00000401338; -.
DR TCDB; 1.N.2.1.6; the myoblast fusion complex (mfc) family.
DR GlyConnect; 1856; 1 N-Linked glycan (1 site).
DR GlyGen; Q9HCN3; 6 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCN3; -.
DR PhosphoSitePlus; Q9HCN3; -.
DR BioMuta; TMEM8A; -.
DR DMDM; 296453013; -.
DR EPD; Q9HCN3; -.
DR jPOST; Q9HCN3; -.
DR MassIVE; Q9HCN3; -.
DR MaxQB; Q9HCN3; -.
DR PaxDb; Q9HCN3; -.
DR PeptideAtlas; Q9HCN3; -.
DR PRIDE; Q9HCN3; -.
DR ProteomicsDB; 81774; -.
DR Antibodypedia; 55489; 20 antibodies from 9 providers.
DR DNASU; 58986; -.
DR Ensembl; ENST00000431232.7; ENSP00000401338.2; ENSG00000129925.11.
DR GeneID; 58986; -.
DR KEGG; hsa:58986; -.
DR MANE-Select; ENST00000431232.7; ENSP00000401338.2; NM_021259.3; NP_067082.2.
DR UCSC; uc002cgu.5; human.
DR CTD; 58986; -.
DR DisGeNET; 58986; -.
DR GeneCards; PGAP6; -.
DR HGNC; HGNC:17205; PGAP6.
DR HPA; ENSG00000129925; Low tissue specificity.
DR MIM; 619342; gene.
DR neXtProt; NX_Q9HCN3; -.
DR OpenTargets; ENSG00000129925; -.
DR PharmGKB; PA38211; -.
DR VEuPathDB; HostDB:ENSG00000129925; -.
DR eggNOG; ENOG502QQ7Q; Eukaryota.
DR GeneTree; ENSGT00940000160060; -.
DR InParanoid; Q9HCN3; -.
DR OMA; PVMREDM; -.
DR OrthoDB; 704708at2759; -.
DR PhylomeDB; Q9HCN3; -.
DR TreeFam; TF331003; -.
DR PathwayCommons; Q9HCN3; -.
DR SignaLink; Q9HCN3; -.
DR BioGRID-ORCS; 58986; 31 hits in 1077 CRISPR screens.
DR ChiTaRS; TMEM8A; human.
DR GenomeRNAi; 58986; -.
DR Pharos; Q9HCN3; Tdark.
DR PRO; PR:Q9HCN3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9HCN3; protein.
DR Bgee; ENSG00000129925; Expressed in body of pancreas and 163 other tissues.
DR ExpressionAtlas; Q9HCN3; baseline and differential.
DR Genevisible; Q9HCN3; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR021910; NGX6/PGAP6/MYMK.
DR PANTHER; PTHR14319; PTHR14319; 1.
DR Pfam; PF12036; DUF3522; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase;
KW Lipid metabolism; Lysosome; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..771
FT /note="Post-GPI attachment to proteins factor 6"
FT /id="PRO_0000022539"
FT TOPO_DOM 35..545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 497..533
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 322..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 498..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 502..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 136
FT /note="T -> A (in dbSNP:rs11248931)"
FT /evidence="ECO:0000269|PubMed:11006113,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_025307"
FT VARIANT 310
FT /note="I -> V (in dbSNP:rs2071915)"
FT /evidence="ECO:0000269|PubMed:11006113,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_025308"
FT VARIANT 567
FT /note="R -> W (in dbSNP:rs3743887)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057810"
FT MUTAGEN 584
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:27881714"
FT MUTAGEN 588
FT /note="H->A: Abolishes shedding of TDGF1."
FT /evidence="ECO:0000269|PubMed:27881714"
FT MUTAGEN 610
FT /note="D->A: Abolishes shedding of TDGF1."
FT /evidence="ECO:0000269|PubMed:27881714"
FT MUTAGEN 722
FT /note="H->A: Abolishes shedding of TDGF1."
FT /evidence="ECO:0000269|PubMed:27881714"
FT MUTAGEN 726
FT /note="H->A: Abolishes shedding of TDGF1."
FT /evidence="ECO:0000269|PubMed:27881714"
FT CONFLICT 460
FT /note="P -> A (in Ref. 6; BAB14975)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="G -> D (in Ref. 1; BAB16376)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="S -> L (in Ref. 6; BAB14975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 771 AA; 84761 MW; 2A21814C449724F8 CRC64;
MGRAGTGTGG EAVAAVVAGP LLLLLLARPP PASAGYSGKS EVGLVSEHFS QAPQRLSFYS
WYGSARLFRF RVPPDAVLLR WLLQVSRESG AACTDAEITV HFRSGAPPVI NPLGTSFPDD
TAVQPSFQVG VPLSTTPRSN ASVNVSHPAP GDWFVAAHLP PSSQKIELKG LAPTCAYVFQ
PELLVTRVVE ISIMEPDVPL PQTLLSHPSY LKVFVPDYTR ELLLELRDCV SNGSLGCPVR
LTVGPVTLPS NFQKVLTCTG APWPCRLLLP SPPWDRWLQV TAESLVGPLG TVAFSAVAAL
TACRPRSVTI QPLLQSSQNQ SFNASSGLLS PSPDHQDLGR SGRVDRSPFC LTNYPVTRED
MDVVSVHFQP LDRVSVRVCS DTPSVMRLRL NTGMDSGGSL TISLRANKTE MRNETVVVAC
VNAASPFLGF NTSLNCTTAF FQGYPLSLSA WSRRANLIIP YPETDNWYLS LQLMCPENAE
DCEQAVVHVE TTLYLVPCLN DCGPYGQCLL LRRHSYLYAS CSCKAGWRGW SCTDNSTAQT
VAQQRAATLL LTLSNLMFLA PIAVSVRRFF LVEASVYAYT MFFSTFYHAC DQPGEAVLCI
LSYDTLQYCD FLGSGAAIWV TILCMARLKT VLKYVLFLLG TLVIAMSLQL DRRGMWNMLG
PCLFAFVIMA SMWAYRCGHR RQCYPTSWQR WAFYLLPGVS MASVGIAIYT SMMTSDNYYY
THSIWHILLA GSAALLLPPP DQPAEPWACS QKFPCHYQIC KNDREELYAV T
