DLGP1_HUMAN
ID DLGP1_HUMAN Reviewed; 977 AA.
AC O14490; A8MWN8; B2RMU8; B7WPA1; B7Z2H2; B7Z2I2; B7Z9Y4; O14489; P78335;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Disks large-associated protein 1;
DE Short=DAP-1;
DE AltName: Full=Guanylate kinase-associated protein;
DE Short=hGKAP;
DE AltName: Full=PSD-95/SAP90-binding protein 1;
DE AltName: Full=SAP90/PSD-95-associated protein 1;
DE Short=SAPAP1;
GN Name=DLGAP1; Synonyms=DAP1, GKAP;
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 1 AND 2).
RC TISSUE=Brain;
RX PubMed=9286858; DOI=10.1046/j.1365-2443.1997.1310329.x;
RA Satoh K., Yanai H., Senda T., Kohu K., Nakamura T., Okumura N.,
RA Matsumine A., Kobayashi S., Toyoshima K., Akiyama T.;
RT "DAP-1, a novel protein that interacts with the guanylate kinase-like
RT domains of hDLG and PSD-95.";
RL Genes Cells 2:415-424(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9024696; DOI=10.1083/jcb.136.3.669;
RA Kim E., Naisbitt S., Hsueh Y.-P., Rao A., Rothschild A., Craig A.M.,
RA Sheng M.;
RT "GKAP, a novel synaptic protein that interacts with the guanylate kinase-
RT like domain of the PSD-95/SAP90 family of channel clustering molecules.";
RL J. Cell Biol. 136:669-678(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5; 6 AND 7).
RC TISSUE=Brain, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
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).
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).
CC -!- FUNCTION: Part of the postsynaptic scaffold in neuronal cells.
CC -!- SUBUNIT: Interacts with guanylate kinase-like domain of DLG1, DLG2,
CC DLG3, DLG4 and AIP1. Interacts with the PDZ domain of SHANK1, SHANK2
CC and SHANK3. Found in a complex with DLG4 and SHANK1, SHANK2 or SHANK3.
CC Found in a complex with DLG4 and BEGAIN. Interacts with DYL2 and LRFN1
CC (By similarity). Interacts with MPP2 (via the SH3-Guanylate kinase-like
CC sub-module) (By similarity). {ECO:0000250|UniProtKB:P97836,
CC ECO:0000250|UniProtKB:Q9D415}.
CC -!- INTERACTION:
CC O14490; P78352: DLG4; NbExp=6; IntAct=EBI-1753207, EBI-80389;
CC O14490; P62993: GRB2; NbExp=3; IntAct=EBI-1753207, EBI-401755;
CC O14490; P16333: NCK1; NbExp=4; IntAct=EBI-1753207, EBI-389883;
CC O14490; Q62696: Dlg1; Xeno; NbExp=2; IntAct=EBI-1753207, EBI-389325;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=DAP1-alpha;
CC IsoId=O14490-1; Sequence=Displayed;
CC Name=2; Synonyms=DAP1-beta;
CC IsoId=O14490-2; Sequence=VSP_006003, VSP_006004;
CC Name=3;
CC IsoId=O14490-3; Sequence=VSP_006003, VSP_006004, VSP_006005,
CC VSP_006006;
CC Name=4;
CC IsoId=O14490-4; Sequence=VSP_043222, VSP_043223;
CC Name=5;
CC IsoId=O14490-5; Sequence=VSP_043718, VSP_043721, VSP_043722;
CC Name=6;
CC IsoId=O14490-6; Sequence=VSP_043719, VSP_043720, VSP_043721,
CC VSP_043723;
CC Name=7;
CC IsoId=O14490-7; Sequence=VSP_006005, VSP_006006;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- SIMILARITY: Belongs to the SAPAP family. {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; AB000277; BAA23258.1; -; mRNA.
DR EMBL; AB000276; BAA23257.1; -; mRNA.
DR EMBL; U67988; AAC51119.1; -; mRNA.
DR EMBL; AK294717; BAH11858.1; -; mRNA.
DR EMBL; AK294747; BAH11868.1; -; mRNA.
DR EMBL; AK299880; BAH13160.1; -; mRNA.
DR EMBL; AK316099; BAH14470.1; -; mRNA.
DR EMBL; AP002472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01654.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01658.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01659.1; -; Genomic_DNA.
DR EMBL; BC136453; AAI36454.1; -; mRNA.
DR EMBL; BC136454; AAI36455.1; -; mRNA.
DR CCDS; CCDS11836.1; -. [O14490-1]
DR CCDS; CCDS42406.1; -. [O14490-2]
DR CCDS; CCDS56049.1; -. [O14490-3]
DR CCDS; CCDS56050.1; -. [O14490-6]
DR CCDS; CCDS56051.1; -. [O14490-4]
DR CCDS; CCDS56052.1; -. [O14490-5]
DR CCDS; CCDS56053.1; -. [O14490-7]
DR PIR; T00014; T00014.
DR RefSeq; NP_001003809.1; NM_001003809.2. [O14490-2]
DR RefSeq; NP_001229690.1; NM_001242761.1. [O14490-7]
DR RefSeq; NP_001229691.1; NM_001242762.1. [O14490-5]
DR RefSeq; NP_001229692.1; NM_001242763.1.
DR RefSeq; NP_001229693.1; NM_001242764.1. [O14490-4]
DR RefSeq; NP_001229694.1; NM_001242765.1. [O14490-3]
DR RefSeq; NP_001229695.1; NM_001242766.1. [O14490-6]
DR RefSeq; NP_004737.2; NM_004746.3. [O14490-1]
DR PDB; 5YPO; X-ray; 2.29 A; C/D=370-384.
DR PDB; 6TNQ; X-ray; 1.30 A; B/D/F=430-437.
DR PDB; 6TQ0; X-ray; 1.95 A; B/D/F/H/J/L/N/P=483-490.
DR PDBsum; 5YPO; -.
DR PDBsum; 6TNQ; -.
DR PDBsum; 6TQ0; -.
DR AlphaFoldDB; O14490; -.
DR SMR; O14490; -.
DR BioGRID; 114660; 20.
DR CORUM; O14490; -.
DR IntAct; O14490; 13.
DR MINT; O14490; -.
DR STRING; 9606.ENSP00000316377; -.
DR GlyGen; O14490; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O14490; -.
DR PhosphoSitePlus; O14490; -.
DR BioMuta; DLGAP1; -.
DR EPD; O14490; -.
DR MassIVE; O14490; -.
DR PaxDb; O14490; -.
DR PeptideAtlas; O14490; -.
DR PRIDE; O14490; -.
DR ProteomicsDB; 48028; -. [O14490-1]
DR ProteomicsDB; 48029; -. [O14490-2]
DR ProteomicsDB; 48030; -. [O14490-3]
DR ProteomicsDB; 48031; -. [O14490-4]
DR ProteomicsDB; 48032; -. [O14490-5]
DR ProteomicsDB; 48033; -. [O14490-6]
DR ProteomicsDB; 48034; -. [O14490-7]
DR ABCD; O14490; 3 sequenced antibodies.
DR Antibodypedia; 21914; 255 antibodies from 37 providers.
DR DNASU; 9229; -.
DR Ensembl; ENST00000315677.8; ENSP00000316377.3; ENSG00000170579.17. [O14490-1]
DR Ensembl; ENST00000400145.6; ENSP00000383010.2; ENSG00000170579.17. [O14490-3]
DR Ensembl; ENST00000400147.6; ENSP00000383011.2; ENSG00000170579.17. [O14490-2]
DR Ensembl; ENST00000400155.5; ENSP00000383019.1; ENSG00000170579.17. [O14490-4]
DR Ensembl; ENST00000534970.5; ENSP00000437817.1; ENSG00000170579.17. [O14490-5]
DR Ensembl; ENST00000539435.5; ENSP00000446312.1; ENSG00000170579.17. [O14490-6]
DR Ensembl; ENST00000581527.5; ENSP00000463864.1; ENSG00000170579.17. [O14490-7]
DR Ensembl; ENST00000581699.5; ENSP00000462848.1; ENSG00000170579.17. [O14490-4]
DR GeneID; 9229; -.
DR KEGG; hsa:9229; -.
DR MANE-Select; ENST00000315677.8; ENSP00000316377.3; NM_004746.4; NP_004737.2.
DR UCSC; uc002kme.3; human. [O14490-1]
DR CTD; 9229; -.
DR DisGeNET; 9229; -.
DR GeneCards; DLGAP1; -.
DR HGNC; HGNC:2905; DLGAP1.
DR HPA; ENSG00000170579; Tissue enriched (brain).
DR MIM; 605445; gene.
DR neXtProt; NX_O14490; -.
DR OpenTargets; ENSG00000170579; -.
DR PharmGKB; PA27361; -.
DR VEuPathDB; HostDB:ENSG00000170579; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000156220; -.
DR HOGENOM; CLU_010880_3_0_1; -.
DR InParanoid; O14490; -.
DR OMA; AYMDGGP; -.
DR OrthoDB; 285447at2759; -.
DR PhylomeDB; O14490; -.
DR TreeFam; TF321382; -.
DR PathwayCommons; O14490; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; O14490; -.
DR SIGNOR; O14490; -.
DR BioGRID-ORCS; 9229; 13 hits in 1062 CRISPR screens.
DR ChiTaRS; DLGAP1; human.
DR GeneWiki; DLGAP1; -.
DR GenomeRNAi; 9229; -.
DR Pharos; O14490; Tbio.
DR PRO; PR:O14490; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O14490; protein.
DR Bgee; ENSG00000170579; Expressed in Brodmann (1909) area 23 and 162 other tissues.
DR ExpressionAtlas; O14490; baseline and differential.
DR Genevisible; O14490; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR InterPro; IPR030524; DLGAP1.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF7; PTHR12353:SF7; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..977
FT /note="Disks large-associated protein 1"
FT /id="PRO_0000174288"
FT REGION 150..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..661
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000250"
FT REGION 672..683
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000250"
FT REGION 899..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 975..977
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97836"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT VAR_SEQ 1..302
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9024696,
FT ECO:0000303|PubMed:9286858"
FT /id="VSP_006003"
FT VAR_SEQ 1..31
FT /note="MKGLSGSRSHHHGVTCDSACDSLSHHSDRKP -> MDLKTLKLFNSQLRCGW
FT LLYIWNKAFMAHLR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043718"
FT VAR_SEQ 1..24
FT /note="MKGLSGSRSHHHGVTCDSACDSLS -> MIDLFKAEWVSSVCVQVSRNGRTD
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043222"
FT VAR_SEQ 1..17
FT /note="MKGLSGSRSHHHGVTCD -> MNLIFHKDILFGIPANK (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043719"
FT VAR_SEQ 18..31
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043720"
FT VAR_SEQ 25..318
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043223"
FT VAR_SEQ 32..319
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043721"
FT VAR_SEQ 303..319
FT /note="MVKSESCQQERSCQYLQ -> MNLIFHKDILFGIPANK (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9024696,
FT ECO:0000303|PubMed:9286858"
FT /id="VSP_006004"
FT VAR_SEQ 530..557
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043722"
FT VAR_SEQ 530
FT /note="T -> TGVIKLSSAVE (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043723"
FT VAR_SEQ 909..929
FT /note="ERRAPPPVPKKPAKGPAPLIR -> VEQCRFCMVHLKTCTNTGQSK (in
FT isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9024696"
FT /id="VSP_006005"
FT VAR_SEQ 930..977
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9024696"
FT /id="VSP_006006"
FT VARIANT 816
FT /note="R -> Q (in dbSNP:rs35822832)"
FT /id="VAR_053648"
FT CONFLICT 734
FT /note="A -> P (in Ref. 2; AAC51119)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="S -> T (in Ref. 2; AAC51119)"
FT /evidence="ECO:0000305"
FT CONFLICT 752..753
FT /note="AA -> SP (in Ref. 2; AAC51119)"
FT /evidence="ECO:0000305"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:5YPO"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:6TNQ"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6TQ0"
SQ SEQUENCE 977 AA; 108873 MW; 670F72B17D9BE667 CRC64;
MKGLSGSRSH HHGVTCDSAC DSLSHHSDRK PYLLSPVEHH PADHPYYTQR NSFQAECVGP
FSDPLASSTF PRRHYTSQQE LKDECALVPR TLATKANRIP ANLLDQFERQ LPLSRDGYHT
LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DEAQAARYGK
RSKSKERRAE PKARPSTSPG WWSSDDNLDG DMCIYHAPSG VMTMGRCPDR SASQYFLEAY
NTISEQAVKA SRSNNDVKCS TCANLPVSLD TPLLKKSAWS STLTVSRARE VYQKASVNMD
QAMVKSESCQ QERSCQYLQV PQDEWTGYTP RGKDDEIPCR RMRSGSYIKA MGDEDSGDSD
TSPKPSPKVA ARRESYLKAT QPSLTELTTL KISNEHSPKL QIRSHSYLRA VSEVSINRSL
DSLDPAGLLT SPKFRSRNES YMRAMSTISQ VSEMEVNGQF ESVCESVFSE LESQAVEALD
LPMPGCFRMR SHSYVRAIEK GCSQDDECVS LRSSSPPRTT TTVRTIQSST VSSCITTYKK
TPPPVPPRTT TKPFISITAQ SSTESAQDAY MDGQGQRGDI ISQSGLSNST ESLDSMKALT
AAIEAANAQI HGPASQHMGN NTATVTTTTT IATVTTEDRK KDHFKKNRCL SIGIQVDDAE
EPDKTGENKA PSKFQSVGVQ VEEEKCFRRF TRSNSVTTAV QADLDFHDNL ENSLESIEDN
SCPGPMARQF SRDASTSTVS IQGSGNHYHA CAADDDFDTD FDPSILPPPD PWIDSITEDP
LEAVQRSVCH RDGHWFLKLL QAERDRMEGW CQQMEREERE NNLPEDILGK IRTAVGSAQL
LMAQKFYQFR ELCEENLNPN AHPRPTSQDL AGFWDMLQLS IENISMKFDE LHQLKANNWK
QMDPLDKKER RAPPPVPKKP AKGPAPLIRE RSLESSQRQE ARKRLMAAKR AASVRQNSAT
ESAESIEIYI PEAQTRL
