DLGP4_HUMAN
ID DLGP4_HUMAN Reviewed; 992 AA.
AC Q9Y2H0; E1P5T5; Q5QPG4; Q5T2Y4; Q5T2Y5; Q9H137; Q9H138; Q9H1L7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Disks large-associated protein 4;
DE Short=DAP-4;
DE AltName: Full=PSD-95/SAP90-binding protein 4;
DE AltName: Full=SAP90/PSD-95-associated protein 4;
DE Short=SAPAP-4;
GN Name=DLGAP4; Synonyms=DAP4, KIAA0964, SAPAP4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=PNS;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-915, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665; SER-744; THR-915 AND
RP SER-973, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in the molecular organization of synapses and
CC neuronal cell signaling. Could be an adapter protein linking ion
CC channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-
CC 95/SAP90 at the plasma membrane.
CC -!- SUBUNIT: Interacts with DLG1 and DLG4/PSD-95. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y2H0; O00499: BIN1; NbExp=4; IntAct=EBI-722139, EBI-719094;
CC Q9Y2H0; P62993: GRB2; NbExp=2; IntAct=EBI-722139, EBI-401755;
CC Q9Y2H0; P16333: NCK1; NbExp=5; IntAct=EBI-722139, EBI-389883;
CC Q9Y2H0; P27986: PIK3R1; NbExp=2; IntAct=EBI-722139, EBI-79464;
CC Q9Y2H0-1; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12000556, EBI-11096309;
CC Q9Y2H0-1; Q8IZ83: ALDH16A1; NbExp=3; IntAct=EBI-12000556, EBI-1044483;
CC Q9Y2H0-1; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12000556, EBI-1166928;
CC Q9Y2H0-1; Q13643: FHL3; NbExp=3; IntAct=EBI-12000556, EBI-741101;
CC Q9Y2H0-1; Q5TD97: FHL5; NbExp=3; IntAct=EBI-12000556, EBI-750641;
CC Q9Y2H0-1; O75344: FKBP6; NbExp=3; IntAct=EBI-12000556, EBI-744771;
CC Q9Y2H0-1; P06241-3: FYN; NbExp=3; IntAct=EBI-12000556, EBI-10691738;
CC Q9Y2H0-1; P43360: MAGEA6; NbExp=3; IntAct=EBI-12000556, EBI-1045155;
CC Q9Y2H0-1; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-12000556, EBI-2514004;
CC Q9Y2H0-1; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12000556, EBI-11522433;
CC Q9Y2H0-1; P16333: NCK1; NbExp=3; IntAct=EBI-12000556, EBI-389883;
CC Q9Y2H0-1; O43639: NCK2; NbExp=6; IntAct=EBI-12000556, EBI-713635;
CC Q9Y2H0-1; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-12000556, EBI-2513978;
CC Q9Y2H0-1; O14745: SLC9A3R1; NbExp=3; IntAct=EBI-12000556, EBI-349787;
CC Q9Y2H0-1; Q15599: SLC9A3R2; NbExp=3; IntAct=EBI-12000556, EBI-1149760;
CC Q9Y2H0-1; O94875-10: SORBS2; NbExp=3; IntAct=EBI-12000556, EBI-12037893;
CC Q9Y2H0-1; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-12000556, EBI-7353612;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2H0-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2H0-1; Sequence=VSP_006013;
CC Name=3;
CC IsoId=Q9Y2H0-3; Sequence=VSP_034910, VSP_034911;
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76808.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023181; BAA76808.2; ALT_INIT; mRNA.
DR EMBL; AL390374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76140.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76135.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76136.1; -; Genomic_DNA.
DR EMBL; BC108706; AAI08707.1; -; mRNA.
DR EMBL; BC153874; AAI53875.1; -; mRNA.
DR CCDS; CCDS13274.1; -. [Q9Y2H0-1]
DR CCDS; CCDS13275.1; -. [Q9Y2H0-3]
DR RefSeq; NP_001035951.1; NM_001042486.3.
DR RefSeq; NP_055717.2; NM_014902.5. [Q9Y2H0-1]
DR RefSeq; NP_892118.1; NM_183006.3. [Q9Y2H0-3]
DR RefSeq; XP_011526990.1; XM_011528688.2.
DR AlphaFoldDB; Q9Y2H0; -.
DR SMR; Q9Y2H0; -.
DR BioGRID; 116513; 77.
DR IntAct; Q9Y2H0; 47.
DR MINT; Q9Y2H0; -.
DR STRING; 9606.ENSP00000363023; -.
DR GlyGen; Q9Y2H0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2H0; -.
DR PhosphoSitePlus; Q9Y2H0; -.
DR SwissPalm; Q9Y2H0; -.
DR BioMuta; DLGAP4; -.
DR DMDM; 205831580; -.
DR EPD; Q9Y2H0; -.
DR jPOST; Q9Y2H0; -.
DR MassIVE; Q9Y2H0; -.
DR MaxQB; Q9Y2H0; -.
DR PaxDb; Q9Y2H0; -.
DR PeptideAtlas; Q9Y2H0; -.
DR PRIDE; Q9Y2H0; -.
DR ProteomicsDB; 85777; -. [Q9Y2H0-2]
DR ProteomicsDB; 85778; -. [Q9Y2H0-1]
DR ProteomicsDB; 85779; -. [Q9Y2H0-3]
DR Antibodypedia; 26505; 123 antibodies from 26 providers.
DR DNASU; 22839; -.
DR Ensembl; ENST00000339266.10; ENSP00000341633.5; ENSG00000080845.19. [Q9Y2H0-2]
DR Ensembl; ENST00000340491.8; ENSP00000345700.4; ENSG00000080845.19. [Q9Y2H0-3]
DR Ensembl; ENST00000373907.6; ENSP00000363014.2; ENSG00000080845.19. [Q9Y2H0-2]
DR Ensembl; ENST00000373913.7; ENSP00000363023.3; ENSG00000080845.19. [Q9Y2H0-1]
DR GeneID; 22839; -.
DR KEGG; hsa:22839; -.
DR MANE-Select; ENST00000339266.10; ENSP00000341633.5; NM_001365621.2; NP_001352550.1.
DR UCSC; uc002xff.4; human. [Q9Y2H0-2]
DR CTD; 22839; -.
DR DisGeNET; 22839; -.
DR GeneCards; DLGAP4; -.
DR HGNC; HGNC:24476; DLGAP4.
DR HPA; ENSG00000080845; Low tissue specificity.
DR MIM; 616191; gene.
DR neXtProt; NX_Q9Y2H0; -.
DR OpenTargets; ENSG00000080845; -.
DR PharmGKB; PA134891458; -.
DR VEuPathDB; HostDB:ENSG00000080845; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000155308; -.
DR HOGENOM; CLU_010880_0_0_1; -.
DR InParanoid; Q9Y2H0; -.
DR OMA; QDLSCHY; -.
DR OrthoDB; 285447at2759; -.
DR PhylomeDB; Q9Y2H0; -.
DR TreeFam; TF321382; -.
DR PathwayCommons; Q9Y2H0; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q9Y2H0; -.
DR SIGNOR; Q9Y2H0; -.
DR BioGRID-ORCS; 22839; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; DLGAP4; human.
DR GeneWiki; DLGAP4; -.
DR GenomeRNAi; 22839; -.
DR Pharos; Q9Y2H0; Tbio.
DR PRO; PR:Q9Y2H0; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y2H0; protein.
DR Bgee; ENSG00000080845; Expressed in cortical plate and 193 other tissues.
DR ExpressionAtlas; Q9Y2H0; baseline and differential.
DR Genevisible; Q9Y2H0; HS.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR InterPro; IPR030527; DLGAP4.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF19; PTHR12353:SF19; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..992
FT /note="Disks large-associated protein 4"
FT /id="PRO_0000174297"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97839"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97839"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..539
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034910"
FT VAR_SEQ 540..550
FT /note="GSLSNSRTLPS -> MALCLELLKQC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034911"
FT VAR_SEQ 671..700
FT /note="VDCIQPVPKEEPSPATKFQSIGVQVEDDWR -> ERTRRNGSHLSEDNGPKA
FT IDVMAPSSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_006013"
FT VARIANT 486
FT /note="A -> T (in dbSNP:rs6019652)"
FT /id="VAR_057716"
FT VARIANT 861
FT /note="R -> Q (in dbSNP:rs2275807)"
FT /id="VAR_057717"
FT CONFLICT 229
FT /note="T -> I (in Ref. 1; BAA76808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 992 AA; 108012 MW; F0EBFBE0DE1AC814 CRC64;
MKGLGDSRPR HLSDSLDPPH EPLFAGTDRN PYLLSPTEAF AREARFPGQN TLPGDGLFPL
NNQLPPPSST FPRIHYNSHF EVPEESPFPS HAQATKINRL PANLLDQFEK QLPIHRDGFS
TLQFPRGEAK ARGESPGRIR HLVHSVQRLF FTKAPSLEGT AGKVGGNGSK KGGMEDGKGR
RAKSKERAKA GEPKRRSRSN ISGWWSSDDN LDGEAGAFRS SGPASGLMTL GRQAERSQPR
YFMHAYNTIS GHMLKTTKNN TTELTAPPPP PAPPATCPSL GVGTDTNYVK RGSWSTLTLS
HAHEVCQKTS ATLDKSLLKS KSCHQGLAYH YLQVPGGGGE WSTTLLSPRE TDAAAEGPIP
CRRMRSGSYI KAMGDEDSDE SGGSPKPSPK TAARRQSYLR ATQQSLGEQS NPRRSLDRLD
SVDMLLPSKC PSWEEDYTPV SDSLNDSSCI SQIFGQASLI PQLFGHEQQV REAELSDQYE
AACESACSEA ESTAAETLDL PLPSYFRSRS HSYLRAIQAG CSQEEDSVSL QSLSPPPSTG
SLSNSRTLPS SSCLVAYKKT PPPVPPRTTS KPFISVTVQS STESAQDTYL DSQDHKSEVT
SQSGLSNSSD SLDSSTRPPS VTRGGVAPAP EAPEPPPKHA ALKSEQGTLT SSESHPEAAP
KRKLSSIGIQ VDCIQPVPKE EPSPATKFQS IGVQVEDDWR SSVPSHSMSS RRDTDSDTQD
ANDSSCKSSE RSLPDCTPHP NSISIDAGPR QAPKIAQIKR NLSYGDNSDP ALEASSLPPP
DPWLETSSSS PAEPAQPGAC RRDGYWFLKL LQAETERLEG WCCQMDKETK ENNLSEEVLG
KVLSAVGSAQ LLMSQKFQQF RGLCEQNLNP DANPRPTAQD LAGFWDLLQL SIEDISMKFD
ELYHLKANSW QLVETPEKRK EEKKPPPPVP KKPAKSKPAV SRDKASDASD KQRQEARKRL
LAAKRAASVR QNSATESADS IEIYVPEAQT RL
