ID ADA22_HUMAN Reviewed; 906 AA. AC Q9P0K1; O75075; O75076; Q9P0K2; Q9UIA1; Q9UKK2; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 207. DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22; DE Short=ADAM 22; DE AltName: Full=Metalloproteinase-disintegrin ADAM22-3; DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2; DE Flags: Precursor; GN Name=ADAM22; Synonyms=MDC2; 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 3 AND 4). RC TISSUE=Brain; RX PubMed=9693107; DOI=10.1042/bj3340093; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and RT MDC3: novel human cellular disintegrins highly expressed in the brain."; RL Biochem. J. 334:93-98(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11050470; DOI=10.1111/j.1349-7006.2000.tb00877.x; RA Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., RA Kuwano M., Wada M.; RT "The specific expression of three novel splice variant forms of human RT metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in brain RT tissues and gliomas."; RL Jpn. J. Cancer Res. 91:1001-1006(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT ARG-81. RC TISSUE=Brain; RA Wada M., Torigoe K., Harada T., Kuwano M.; RT "Isolation and tissue specific expression of novel ADAM family from 7q21.1 RT region."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-906 (ISOFORM 1), AND VARIANT ARG-81. RC TISSUE=Cerebellum; RX PubMed=10524237; DOI=10.1016/s0378-1119(99)00302-9; RA Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.; RT "The identification of seven metalloproteinase-disintegrin (ADAM) genes RT from genomic libraries."; RL Gene 237:61-70(1999). RN [6] RP FUNCTION, INTERACTION WITH YWHAZ, AND MUTAGENESIS OF SER-834 AND SER-857. RX PubMed=12589811; DOI=10.1016/s0006-291x(03)00056-1; RA Zhu P., Sun Y., Xu R., Sang Y., Zhao J., Liu G., Cai L., Li C., Zhao S.; RT "The interaction between ADAM 22 and 14-3-3zeta: regulation of cell RT adhesion and spreading."; RL Biochem. Biophys. Res. Commun. 301:991-999(2003). RN [7] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [8] RP FUNCTION, INTERACTION WITH YWHAB, AND MUTAGENESIS OF SER-834 AND SER-857. RX PubMed=15882968; DOI=10.1016/j.bbrc.2005.03.229; RA Zhu P., Sang Y., Xu H., Zhao J., Xu R., Sun Y., Xu T., Wang X., Chen L., RA Feng H., Li C., Zhao S.; RT "ADAM22 plays an important role in cell adhesion and spreading with the RT assistance of 14-3-3."; RL Biochem. Biophys. Res. Commun. 331:938-946(2005). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16385342; DOI=10.1227/01.neu.0000192363.84287.8b; RA D'Abaco G.M., Ng K., Paradiso L., Godde N.J., Kaye A., Novak U.; RT "ADAM22, expressed in normal brain but not in high-grade gliomas, inhibits RT cellular proliferation via the disintegrin domain."; RL Neurosurgery 58:179-186(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, 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 [11] RP INVOLVEMENT IN DEE61, VARIANT DEE61 TYR-401, INTERACTION WITH LGI1 AND RP DLG4, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT DEE61 TYR-401. RX PubMed=27066583; DOI=10.1212/nxg.0000000000000046; RA Muona M., Fukata Y., Anttonen A.K., Laari A., Palotie A., Pihko H., RA Loennqvist T., Valanne L., Somer M., Fukata M., Lehesjoki A.E.; RT "Dysfunctional ADAM22 implicated in progressive encephalopathy with RT cortical atrophy and epilepsy."; RL Neurol. Genet. 2:E46-E46(2016). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION AT RP ASN-519; ASN-634 AND ASN-675, DISULFIDE BONDS, AND FUNCTION. RX PubMed=19692335; DOI=10.1074/jbc.m109.014258; RA Liu H., Shim A.H., He X.; RT "Structural characterization of the ectodomain of a disintegrin and RT metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of RT metalloproteinase: insights on ADAM function."; RL J. Biol. Chem. 284:29077-29086(2009). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein (PubMed:19692335). Involved in CC regulation of cell adhesion and spreading and in inhibition of cell CC proliferation. Neuronal receptor for LGI1. CC {ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:15882968, CC ECO:0000269|PubMed:16385342, ECO:0000269|PubMed:19692335}. CC -!- SUBUNIT: Interacts with LGI1 (PubMed:27066583). Interacts with CC DLG4/PSD95 (PubMed:27066583). Also binds LGI4 (By similarity). CC Interacts with KCNA2 and DLG2 (By similarity). Interacts with ADAM11 CC (By similarity). Interacts (via C-terminus) with YWHAB/14-3-3 beta CC (PubMed:15882968). Interacts (via C-terminus) with YWHAZ/14-3-3 zeta CC (PubMed:12589811). {ECO:0000250|UniProtKB:Q9R1V6, CC ECO:0000269|PubMed:12589811, ECO:0000269|PubMed:15882968, CC ECO:0000269|PubMed:27066583}. CC -!- INTERACTION: CC Q9P0K1; Q14160: SCRIB; NbExp=3; IntAct=EBI-1567236, EBI-357345; CC Q9P0K1; P63104: YWHAZ; NbExp=3; IntAct=EBI-1567236, EBI-347088; CC Q9P0K1-3; P31946: YWHAB; NbExp=2; IntAct=EBI-1567267, EBI-359815; CC Q9P0K1-3; P27348: YWHAQ; NbExp=2; IntAct=EBI-1567267, EBI-359854; CC Q9P0K1-3; P63104: YWHAZ; NbExp=3; IntAct=EBI-1567267, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27066583}; CC Single-pass type I membrane protein {ECO:0000305}. Cell projection, CC axon {ECO:0000250|UniProtKB:Q9R1V6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Epsilon; CC IsoId=Q9P0K1-1; Sequence=Displayed; CC Name=2; Synonyms=Delta; CC IsoId=Q9P0K1-2; Sequence=VSP_005482, VSP_005484; CC Name=3; Synonyms=Alpha; CC IsoId=Q9P0K1-3; Sequence=VSP_005483; CC Name=4; Synonyms=Beta; CC IsoId=Q9P0K1-4; Sequence=VSP_005482, VSP_005483; CC Name=5; CC IsoId=Q9P0K1-5; Sequence=VSP_005482; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and in some high- CC grade but not low-grade gliomas. Detected slightly or not at all in CC other tissues. {ECO:0000269|PubMed:16385342}. CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. CC -!- DISEASE: Developmental and epileptic encephalopathy 61 (DEE61) CC [MIM:617933]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE61 is an autosomal recessive condition CC characterized by onset of seizures in infancy. CC {ECO:0000269|PubMed:27066583}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {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; AB009671; BAA32349.1; -; mRNA. DR EMBL; AB009671; BAA32350.1; -; mRNA. DR EMBL; AF155381; AAF73288.1; -; mRNA. DR EMBL; AF155382; AAF73289.1; -; mRNA. DR EMBL; AF073291; AAF22476.2; -; mRNA. DR EMBL; AC005075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF158637; AAD55251.1; -; mRNA. DR CCDS; CCDS43608.1; -. [Q9P0K1-2] DR CCDS; CCDS43609.1; -. [Q9P0K1-5] DR CCDS; CCDS43610.1; -. [Q9P0K1-3] DR CCDS; CCDS47637.1; -. [Q9P0K1-1] DR CCDS; CCDS94138.1; -. [Q9P0K1-4] DR RefSeq; NP_004185.1; NM_004194.4. [Q9P0K1-3] DR RefSeq; NP_068367.1; NM_021721.4. [Q9P0K1-4] DR RefSeq; NP_068368.2; NM_021722.5. [Q9P0K1-2] DR RefSeq; NP_068369.1; NM_021723.4. [Q9P0K1-1] DR PDB; 3G5C; X-ray; 2.36 A; A/B=233-736. DR PDB; 5Y2Z; X-ray; 2.67 A; A/C/E/G/I/K=233-729. DR PDB; 5Y31; X-ray; 7.12 A; A/C=233-729. DR PDB; 7CQF; X-ray; 1.80 A; A=892-906. DR PDBsum; 3G5C; -. DR PDBsum; 5Y2Z; -. DR PDBsum; 5Y31; -. DR PDBsum; 7CQF; -. DR AlphaFoldDB; Q9P0K1; -. DR SMR; Q9P0K1; -. DR BioGRID; 119789; 25. DR CORUM; Q9P0K1; -. DR ELM; Q9P0K1; -. DR IntAct; Q9P0K1; 16. DR MINT; Q9P0K1; -. DR STRING; 9606.ENSP00000265727; -. DR MEROPS; M12.978; -. DR GlyCosmos; Q9P0K1; 4 sites, No reported glycans. DR GlyGen; Q9P0K1; 4 sites. DR iPTMnet; Q9P0K1; -. DR PhosphoSitePlus; Q9P0K1; -. DR BioMuta; ADAM22; -. DR DMDM; 14423634; -. DR EPD; Q9P0K1; -. DR jPOST; Q9P0K1; -. DR MassIVE; Q9P0K1; -. DR MaxQB; Q9P0K1; -. DR PaxDb; 9606-ENSP00000265727; -. DR PeptideAtlas; Q9P0K1; -. DR ProteomicsDB; 83556; -. [Q9P0K1-1] DR ProteomicsDB; 83557; -. [Q9P0K1-2] DR ProteomicsDB; 83558; -. [Q9P0K1-3] DR ProteomicsDB; 83559; -. [Q9P0K1-4] DR ProteomicsDB; 83560; -. [Q9P0K1-5] DR Pumba; Q9P0K1; -. DR Antibodypedia; 29782; 354 antibodies from 26 providers. DR DNASU; 53616; -. DR Ensembl; ENST00000265727.11; ENSP00000265727.7; ENSG00000008277.15. [Q9P0K1-1] DR Ensembl; ENST00000398201.8; ENSP00000381260.4; ENSG00000008277.15. [Q9P0K1-3] DR Ensembl; ENST00000398204.8; ENSP00000381262.4; ENSG00000008277.15. [Q9P0K1-5] DR Ensembl; ENST00000398209.7; ENSP00000381267.3; ENSG00000008277.15. [Q9P0K1-2] DR Ensembl; ENST00000684002.1; ENSP00000508320.1; ENSG00000008277.15. [Q9P0K1-4] DR GeneID; 53616; -. DR KEGG; hsa:53616; -. DR UCSC; uc003ujk.3; human. [Q9P0K1-1] DR AGR; HGNC:201; -. DR CTD; 53616; -. DR DisGeNET; 53616; -. DR GeneCards; ADAM22; -. DR HGNC; HGNC:201; ADAM22. DR HPA; ENSG00000008277; Tissue enriched (brain). DR MalaCards; ADAM22; -. DR MIM; 603709; gene. DR MIM; 617933; phenotype. DR neXtProt; NX_Q9P0K1; -. DR OpenTargets; ENSG00000008277; -. DR PharmGKB; PA24518; -. DR VEuPathDB; HostDB:ENSG00000008277; -. DR eggNOG; KOG3607; Eukaryota. DR GeneTree; ENSGT00940000156889; -. DR InParanoid; Q9P0K1; -. DR OMA; TAWGYNM; -. DR OrthoDB; 5406290at2759; -. DR PhylomeDB; Q9P0K1; -. DR TreeFam; TF314733; -. DR PathwayCommons; Q9P0K1; -. DR Reactome; R-HSA-5682910; LGI-ADAM interactions. DR SignaLink; Q9P0K1; -. DR BioGRID-ORCS; 53616; 8 hits in 1150 CRISPR screens. DR ChiTaRS; ADAM22; human. DR EvolutionaryTrace; Q9P0K1; -. DR GeneWiki; ADAM22; -. DR GenomeRNAi; 53616; -. DR Pharos; Q9P0K1; Tbio. DR PRO; PR:Q9P0K1; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9P0K1; Protein. DR Bgee; ENSG00000008277; Expressed in lateral nuclear group of thalamus and 157 other cell types or tissues. DR ExpressionAtlas; Q9P0K1; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005178; F:integrin binding; NAS:UniProtKB. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 4.10.70.10; Disintegrin domain; 1. DR Gene3D; 2.10.25.10; Laminin; 1. DR InterPro; IPR006586; ADAM_Cys-rich. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1. DR PANTHER; PTHR11905:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 1. DR Pfam; PF08516; ADAM_CR; 1. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR Genevisible; Q9P0K1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Cell projection; Cleavage on pair of basic residues; Disease variant; KW Disulfide bond; EGF-like domain; Epilepsy; Glycoprotein; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT PROPEP 26..222 FT /evidence="ECO:0000250" FT /id="PRO_0000029112" FT CHAIN 223..906 FT /note="Disintegrin and metalloproteinase domain-containing FT protein 22" FT /id="PRO_0000029113" FT TOPO_DOM 223..736 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 737..757 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 758..906 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 239..438 FT /note="Peptidase M12B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276" FT DOMAIN 444..531 FT /note="Disintegrin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DOMAIN 675..712 FT /note="EGF-like" FT REGION 785..906 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 788..812 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 855..877 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 810 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R1V6" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 857 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R1V6" FT MOD_RES 862 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R1V6" FT MOD_RES 866 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R1V6" FT MOD_RES 870 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R1V6" FT CARBOHYD 175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 519 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19692335" FT CARBOHYD 634 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19692335" FT CARBOHYD 675 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 349..433 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 392..417 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 394..401 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 447..477 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 458..474 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 460..466 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 473..494 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 485..491 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 490..516 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 503..523 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 510..542 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 535..547 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 554..605 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 569..635 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 583..593 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 600..663 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 657..668 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 679..694 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 688..700 FT /evidence="ECO:0000269|PubMed:19692335" FT DISULFID 702..711 FT /evidence="ECO:0000269|PubMed:19692335" FT VAR_SEQ 768..803 FT /note="Missing (in isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11050470, FT ECO:0000303|PubMed:9693107, ECO:0000303|Ref.3" FT /id="VSP_005482" FT VAR_SEQ 859 FT /note="E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11050470" FT /id="VSP_005484" FT VAR_SEQ 860..906 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:9693107" FT /id="VSP_005483" FT VARIANT 81 FT /note="P -> R (in dbSNP:rs2279542)" FT /evidence="ECO:0000269|PubMed:10524237, ECO:0000269|Ref.3" FT /id="VAR_020057" FT VARIANT 119 FT /note="H -> Y (in dbSNP:rs4728730)" FT /id="VAR_051589" FT VARIANT 207 FT /note="V -> I (in dbSNP:rs17255978)" FT /id="VAR_051590" FT VARIANT 401 FT /note="C -> Y (in DEE61; uncertain significance; loss of FT interaction with LGI1; no effect on DLG4-binding, nor on FT subcellular location; dbSNP:rs747259064)" FT /evidence="ECO:0000269|PubMed:27066583" FT /id="VAR_080496" FT MUTAGEN 834 FT /note="S->A: Abolishes interactions with YWHAB and YWHAZ; FT when associated with A-857." FT /evidence="ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968" FT MUTAGEN 857 FT /note="S->A: Abolishes interactions with YWHAB and YWHAZ; FT when associated with A-834." FT /evidence="ECO:0000269|PubMed:12589811, FT ECO:0000269|PubMed:15882968" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 239..247 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 249..253 FT /evidence="ECO:0007829|PDB:3G5C" FT TURN 254..257 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 259..280 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 281..292 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 305..318 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 325..333 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:3G5C" FT TURN 351..353 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 354..359 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 363..378 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 384..389 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:5Y2Z" FT HELIX 416..427 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 432..435 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 463..466 FT /evidence="ECO:0007829|PDB:3G5C" FT TURN 467..473 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 474..479 FT /evidence="ECO:0007829|PDB:5Y2Z" FT STRAND 486..488 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 491..496 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:3G5C" FT TURN 536..539 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 540..543 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 546..548 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 550..558 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 567..573 FT /evidence="ECO:0007829|PDB:3G5C" FT TURN 574..576 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 585..590 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 595..597 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 600..602 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 613..617 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 622..628 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 631..637 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 640..645 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 656..658 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 668..670 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 671..674 FT /evidence="ECO:0007829|PDB:3G5C" FT HELIX 688..690 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 692..695 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 700..702 FT /evidence="ECO:0007829|PDB:3G5C" FT STRAND 706..708 FT /evidence="ECO:0007829|PDB:3G5C" FT CONFLICT Q9P0K1-2:848 FT /note="G -> E (in Ref. 2; AAF73288)" FT /evidence="ECO:0000305" SQ SEQUENCE 906 AA; 100433 MW; 265ECCD0FA6C088B CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI //