PHLD_HUMAN
ID PHLD_HUMAN Reviewed; 840 AA.
AC P80108; Q15127; Q15128; Q2M2F2; Q5T3Y0; Q7Z6T8; Q8TCV0; Q8WW82; Q96ID6;
AC Q9H167; Q9H4M1; Q9UJC9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D;
DE Short=PI-G PLD;
DE EC=3.1.4.50;
DE AltName: Full=Glycoprotein phospholipase D;
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D;
DE Short=GPI-PLD;
DE Short=GPI-specific phospholipase D;
DE Flags: Precursor;
GN Name=GPLD1; Synonyms=PIGPLD1;
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] (ISOFORM 1), AND VARIANTS ILE-30; VAL-350;
RP MET-461 AND ILE-698.
RC TISSUE=Liver, and Pancreas;
RA Tsang T.C., Fung W.-J.C., Levine J., Metz C.N., Davitz M.A., Burns D.K.,
RA Huang K.-S., Kochan J.P.;
RT "Isolation and expression of two human glycosylphosphatidylinositol
RT phospholipase D (GPI-PLD) cDNAs.";
RL FASEB J. 6:A1922-A1922(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 384-840, AND VARIANTS ILE-30; VAL-694 AND ILE-698.
RC TISSUE=Liver;
RX PubMed=11072085; DOI=10.1016/s0167-4781(00)00194-9;
RA Schofield J.N., Rademacher T.W.;
RT "Structure and expression of the human glycosylphosphatidylinositol
RT phospholipase D1 (GPLD1) gene.";
RL Biochim. Biophys. Acta 1494:189-194(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-698.
RC TISSUE=Bone marrow;
RA Tang J.H., Gu S.L., Zhang X.J.;
RT "Preliminary study of the gene structure of human
RT glycosylphosphatidylinositol specific phospholipase D.";
RL Hunan Yi Ke Da Xue Xue Bao 26:96-97(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 266-840 (ISOFORM 1), AND VARIANTS VAL-17; ILE-30 AND
RP ILE-698.
RC TISSUE=Eye, and Liver;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Serum;
RX PubMed=1606959; DOI=10.1111/j.1432-1033.1992.tb16981.x;
RA Hoener M.C., Brodbeck U.;
RT "Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic
RT glycoprotein that in serum is associated with high-density lipoproteins.";
RL Eur. J. Biochem. 206:747-757(1992).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: This protein hydrolyzes the inositol phosphate linkage in
CC proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus
CC releasing these proteins from the membrane.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a
CC 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80108-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80108-2; Sequence=VSP_023261, VSP_023262;
CC -!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36444.1; Type=Miscellaneous discrepancy; Note=This sequence has numerous of conflicts with the human genome.; Evidence={ECO:0000305};
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DR EMBL; L11701; AAA36444.1; ALT_SEQ; mRNA.
DR EMBL; L11702; AAA36445.1; -; mRNA.
DR EMBL; AJ308108; CAC87068.1; -; mRNA.
DR EMBL; AJ400872; CAC14844.1; -; Genomic_DNA.
DR EMBL; AJ400873; CAC14844.1; JOINED; Genomic_DNA.
DR EMBL; AJ400874; CAC14844.1; JOINED; Genomic_DNA.
DR EMBL; AJ400875; CAC14844.1; JOINED; Genomic_DNA.
DR EMBL; AJ400876; CAC14844.1; JOINED; Genomic_DNA.
DR EMBL; AY007546; AAG16627.2; -; mRNA.
DR EMBL; AL359713; CAI17103.1; -; Genomic_DNA.
DR EMBL; AL031230; CAI17103.1; JOINED; Genomic_DNA.
DR EMBL; AL031230; CAI22602.1; -; Genomic_DNA.
DR EMBL; AL359713; CAI22602.1; JOINED; Genomic_DNA.
DR EMBL; AL031230; CAD92520.1; -; Genomic_DNA.
DR EMBL; BC007614; AAH07614.1; -; mRNA.
DR EMBL; BC020748; AAH20748.1; -; mRNA.
DR EMBL; BC093645; AAH93645.1; -; mRNA.
DR EMBL; BC112001; AAI12002.1; -; mRNA.
DR CCDS; CCDS4553.1; -. [P80108-1]
DR RefSeq; NP_001494.2; NM_001503.3. [P80108-1]
DR AlphaFoldDB; P80108; -.
DR BioGRID; 109083; 9.
DR IntAct; P80108; 1.
DR STRING; 9606.ENSP00000230036; -.
DR GlyConnect; 1601; 16 N-Linked glycans (4 sites).
DR GlyGen; P80108; 10 sites, 22 N-linked glycans (4 sites).
DR iPTMnet; P80108; -.
DR PhosphoSitePlus; P80108; -.
DR BioMuta; GPLD1; -.
DR DMDM; 126302583; -.
DR CPTAC; CPTAC-2231; -.
DR jPOST; P80108; -.
DR MassIVE; P80108; -.
DR PaxDb; P80108; -.
DR PeptideAtlas; P80108; -.
DR PRIDE; P80108; -.
DR ProteomicsDB; 57666; -. [P80108-1]
DR ProteomicsDB; 57667; -. [P80108-2]
DR Antibodypedia; 1368; 283 antibodies from 29 providers.
DR DNASU; 2822; -.
DR Ensembl; ENST00000230036.2; ENSP00000230036.1; ENSG00000112293.15. [P80108-1]
DR GeneID; 2822; -.
DR KEGG; hsa:2822; -.
DR MANE-Select; ENST00000230036.2; ENSP00000230036.1; NM_001503.4; NP_001494.2.
DR UCSC; uc003ned.3; human. [P80108-1]
DR CTD; 2822; -.
DR DisGeNET; 2822; -.
DR GeneCards; GPLD1; -.
DR HGNC; HGNC:4459; GPLD1.
DR HPA; ENSG00000112293; Tissue enriched (liver).
DR MalaCards; GPLD1; -.
DR MIM; 602515; gene.
DR neXtProt; NX_P80108; -.
DR OpenTargets; ENSG00000112293; -.
DR PharmGKB; PA28842; -.
DR VEuPathDB; HostDB:ENSG00000112293; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00390000013522; -.
DR HOGENOM; CLU_011756_0_0_1; -.
DR InParanoid; P80108; -.
DR OMA; SQSWFTI; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P80108; -.
DR TreeFam; TF335726; -.
DR BRENDA; 3.1.4.50; 2681.
DR PathwayCommons; P80108; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; P80108; -.
DR BioGRID-ORCS; 2822; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; GPLD1; human.
DR GeneWiki; GPLD1; -.
DR GenomeRNAi; 2822; -.
DR Pharos; P80108; Tbio.
DR PRO; PR:P80108; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P80108; protein.
DR Bgee; ENSG00000112293; Expressed in secondary oocyte and 151 other tissues.
DR Genevisible; P80108; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IDA:UniProtKB.
DR GO; GO:0004630; F:phospholipase D activity; IDA:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; IMP:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
DR GO; GO:0071401; P:cellular response to triglyceride; IMP:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0006507; P:GPI anchor release; IDA:UniProtKB.
DR GO; GO:0035701; P:hematopoietic stem cell migration; TAS:UniProtKB.
DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; TAS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0070633; P:transepithelial transport; ISS:UniProtKB.
DR Gene3D; 2.130.10.130; -; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001028; Gprt_PLipase_D.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR029002; PLPC/GPLD1.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00718; PHPHLIPASED.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lipid metabolism; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..840
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /id="PRO_0000022047"
FT REPEAT 367..428
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 436..497
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 499..559
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 563..623
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 633..693
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 704..770
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 788..840
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 165..176
FT /note="GDVLSQFEFNFN -> TVYLHLLNFLVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023261"
FT VAR_SEQ 177..840
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023262"
FT VARIANT 17
FT /note="L -> V (in dbSNP:rs2235501)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030743"
FT VARIANT 30
FT /note="V -> I (in dbSNP:rs1126617)"
FT /evidence="ECO:0000269|PubMed:11072085,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_030744"
FT VARIANT 275
FT /note="D -> E (in dbSNP:rs17300770)"
FT /id="VAR_030745"
FT VARIANT 350
FT /note="I -> V (in dbSNP:rs1062496)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_051278"
FT VARIANT 396
FT /note="G -> S (in dbSNP:rs6924628)"
FT /id="VAR_030746"
FT VARIANT 461
FT /note="V -> M (in dbSNP:rs1062505)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_030747"
FT VARIANT 694
FT /note="M -> V (in dbSNP:rs1042303)"
FT /evidence="ECO:0000269|PubMed:11072085"
FT /id="VAR_030748"
FT VARIANT 698
FT /note="T -> I (in dbSNP:rs1772256)"
FT /evidence="ECO:0000269|PubMed:11072085,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.3"
FT /id="VAR_030749"
FT CONFLICT 531..534
FT /note="VIGS -> MLGT (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 840 AA; 92336 MW; 11369BAFEC3D6D38 CRC64;
MSAFRLWPGL LIMLGSLCHR GSPCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY
QAGIVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF
GITSHMAADV SWHSLGLEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR
RWYVPVKDLL GIYEKLYGRK VITENVIVDC SHIQFLEMYG EMLAVSKLYP TYSTKSPFLV
EQFQEYFLGG LDDMAFWSTN IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ
KNDFHRNLTT SLTESVDRNI NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL
SQKHVSSPLA SYFLSFPYAR LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHIGRVYLIY
GNDLGLPPVD LDLDKEAHRI LEGFQPSGRF GSALAVLDFN VDGVPDLAVG APSVGSEQLT
YKGAVYVYFG SKQGGMSSSP NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG
GKQKGIVAAF YSGPSLSDKE KLNVEAANWT VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP
TWKNASRLGH LLHIRDEKKS LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG
TLKQVLLVGA PTYDDVSKVA FLTVTLHQGG ATRMYALTSD AQPLLLSTFS GDRRFSRFGG
VLHLSDLDDD GLDEIIMAAP LRIADVTSGL IGGEDGRVYV YNGKETTLGD MTGKCKSWIT
PCPEEKAQYV LISPEASSRF GSSLITVRSK AKNQVVIAAG RSSLGARLSG ALHVYSLGSD
