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   27-MAR-2024, entry version 174.
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 CRIPTO, but not CFC1, at the cell
CC       surface. Shedding of CRIPTO modulates Nodal signaling by allowing
CC       soluble CRIPTO 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   SMR; Q9HCN3; -.
DR   BioGRID; 121856; 29.
DR   IntAct; Q9HCN3; 17.
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   GlyCosmos; Q9HCN3; 5 sites, 2 glycans.
DR   GlyGen; Q9HCN3; 6 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HCN3; -.
DR   PhosphoSitePlus; Q9HCN3; -.
DR   SwissPalm; Q9HCN3; -.
DR   BioMuta; TMEM8A; -.
DR   DMDM; 296453013; -.
DR   EPD; Q9HCN3; -.
DR   jPOST; Q9HCN3; -.
DR   MassIVE; Q9HCN3; -.
DR   MaxQB; Q9HCN3; -.
DR   PaxDb; 9606-ENSP00000401338; -.
DR   PeptideAtlas; Q9HCN3; -.
DR   ProteomicsDB; 81774; -.
DR   Antibodypedia; 55489; 21 antibodies from 10 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   AGR; HGNC:17205; -.
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; SLWANKS; -.
DR   OrthoDB; 1018107at2759; -.
DR   PhylomeDB; Q9HCN3; -.
DR   TreeFam; TF331003; -.
DR   PathwayCommons; Q9HCN3; -.
DR   SignaLink; Q9HCN3; -.
DR   BioGRID-ORCS; 58986; 31 hits in 1151 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 165 other cell types or tissues.
DR   ExpressionAtlas; Q9HCN3; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
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; FIVE-SPAN TRANSMEMBRANE PROTEIN M83; 1.
DR   PANTHER; PTHR14319:SF7; POST-GPI ATTACHMENT TO PROTEINS FACTOR 6; 1.
DR   Pfam; PF12036; DUF3522; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   Genevisible; Q9HCN3; HS.
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 CRIPTO."
FT                   /evidence="ECO:0000269|PubMed:27881714"
FT   MUTAGEN         610
FT                   /note="D->A: Abolishes shedding of CRIPTO."
FT                   /evidence="ECO:0000269|PubMed:27881714"
FT   MUTAGEN         722
FT                   /note="H->A: Abolishes shedding of CRIPTO."
FT                   /evidence="ECO:0000269|PubMed:27881714"
FT   MUTAGEN         726
FT                   /note="H->A: Abolishes shedding of CRIPTO."
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
//