ADA22_HUMAN
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 03-AUG-2022, entry version 198.
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 (via C-
CC terminus) with YWHAB/14-3-3 beta and YWHAZ/14-3-3 zeta but not with
CC YWHAE/14-3-3 epsilon or YWHAH/14-3-3 eta (PubMed:12589811,
CC PubMed:15882968). {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}.
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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 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; 21.
DR CORUM; Q9P0K1; -.
DR ELM; Q9P0K1; -.
DR IntAct; Q9P0K1; 14.
DR MINT; Q9P0K1; -.
DR STRING; 9606.ENSP00000265727; -.
DR MEROPS; M12.978; -.
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; Q9P0K1; -.
DR PeptideAtlas; Q9P0K1; -.
DR PRIDE; 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 Antibodypedia; 29782; 343 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 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; TAWGYKK; -.
DR OrthoDB; 162519at2759; -.
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 1071 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 155 other tissues.
DR ExpressionAtlas; Q9P0K1; baseline and differential.
DR Genevisible; Q9P0K1; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
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; IEA:InterPro.
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; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 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 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; SSF57552; 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.
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; unknown pathological significance;
FT loss of interaction with LGI1; no effect on DLG4-binding,
FT nor on 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
