GenomeNet

Database: UniProt
Entry: Q9P0K1
LinkDB: Q9P0K1
Original site: Q9P0K1 
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   13-FEB-2019, entry version 179.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   and MDC3: novel human cellular disintegrins highly expressed in the
RT   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
RT   brain 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
RT   7q21.1 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.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   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.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., 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)
RT   genes from genomic libraries.";
RL   Gene 237:61-70(1999).
RN   [6]
RP   FUNCTION, INTERACTION WITH YWHAZ, AND MUTAGENESIS OF SER-834 AND
RP   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.,
RA   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
RP   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.,
RA   Chen L., Feng H., Li C., Zhao S.;
RT   "ADAM22 plays an important role in cell adhesion and spreading with
RT   the 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,
RT   inhibits cellular proliferation via the disintegrin domain.";
RL   Neurosurgery 58:179-186(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [11]
RP   INVOLVEMENT IN EIEE61, VARIANT EIEE61 TYR-401, INTERACTION WITH LGI1
RP   AND DLG4, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT EIEE61
RP   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
CC       in regulation of cell adhesion and spreading and in inhibition of
CC       cell 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
CC       with 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       Q14160:SCRIB; NbExp=3; IntAct=EBI-1567236, EBI-357345;
CC       P31946:YWHAB; NbExp=2; IntAct=EBI-1567267, EBI-359815;
CC       P27348:YWHAQ; NbExp=2; IntAct=EBI-1567267, EBI-359854;
CC       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
CC       projection, 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         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.
CC         Ref.2 (AAF73288) sequence is in conflict in position: 848:G->E.
CC         {ECO:0000305};
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
CC       high-grade but not low-grade gliomas. Detected slightly or not at
CC       all in other tissues. {ECO:0000269|PubMed:16385342}.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC       {ECO:0000250}.
CC   -!- DISEASE: Epileptic encephalopathy, early infantile, 61 (EIEE61)
CC       [MIM:617933]: A form of epileptic encephalopathy, a heterogeneous
CC       group of severe childhood onset epilepsies characterized by
CC       refractory seizures, neurodevelopmental impairment, and poor
CC       prognosis. Development is normal prior to seizure onset, after
CC       which cognitive and motor delays become apparent. EIEE61 is an
CC       autosomal recessive condition characterized by onset of seizures
CC       in infancy. {ECO:0000269|PubMed:27066583}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
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   UniGene; Hs.256398; -.
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   PDBsum; 3G5C; -.
DR   PDBsum; 5Y2Z; -.
DR   PDBsum; 5Y31; -.
DR   ProteinModelPortal; Q9P0K1; -.
DR   SMR; Q9P0K1; -.
DR   BioGrid; 119789; 13.
DR   CORUM; Q9P0K1; -.
DR   ELM; Q9P0K1; -.
DR   IntAct; Q9P0K1; 13.
DR   MINT; Q9P0K1; -.
DR   STRING; 9606.ENSP00000265727; -.
DR   MEROPS; M12.978; -.
DR   iPTMnet; Q9P0K1; -.
DR   PhosphoSitePlus; Q9P0K1; -.
DR   BioMuta; ADAM22; -.
DR   DMDM; 14423634; -.
DR   jPOST; Q9P0K1; -.
DR   MaxQB; Q9P0K1; -.
DR   PaxDb; Q9P0K1; -.
DR   PeptideAtlas; Q9P0K1; -.
DR   PRIDE; Q9P0K1; -.
DR   ProteomicsDB; 83556; -.
DR   ProteomicsDB; 83557; -. [Q9P0K1-2]
DR   ProteomicsDB; 83558; -. [Q9P0K1-3]
DR   ProteomicsDB; 83559; -. [Q9P0K1-4]
DR   ProteomicsDB; 83560; -. [Q9P0K1-5]
DR   Ensembl; ENST00000265727; ENSP00000265727; ENSG00000008277. [Q9P0K1-1]
DR   Ensembl; ENST00000398201; ENSP00000381260; ENSG00000008277. [Q9P0K1-3]
DR   Ensembl; ENST00000398204; ENSP00000381262; ENSG00000008277. [Q9P0K1-5]
DR   Ensembl; ENST00000398209; ENSP00000381267; ENSG00000008277. [Q9P0K1-2]
DR   GeneID; 53616; -.
DR   KEGG; hsa:53616; -.
DR   UCSC; uc003ujk.3; human. [Q9P0K1-1]
DR   CTD; 53616; -.
DR   DisGeNET; 53616; -.
DR   EuPathDB; HostDB:ENSG00000008277.14; -.
DR   GeneCards; ADAM22; -.
DR   HGNC; HGNC:201; ADAM22.
DR   HPA; HPA050325; -.
DR   MalaCards; ADAM22; -.
DR   MIM; 603709; gene.
DR   MIM; 617933; phenotype.
DR   neXtProt; NX_Q9P0K1; -.
DR   OpenTargets; ENSG00000008277; -.
DR   PharmGKB; PA24518; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000156889; -.
DR   HOGENOM; HOG000231962; -.
DR   HOVERGEN; HBG050456; -.
DR   InParanoid; Q9P0K1; -.
DR   KO; K16068; -.
DR   OMA; SWQGNIG; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9P0K1; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-HSA-5682910; LGI-ADAM interactions.
DR   ChiTaRS; ADAM22; human.
DR   EvolutionaryTrace; Q9P0K1; -.
DR   GeneWiki; ADAM22; -.
DR   GenomeRNAi; 53616; -.
DR   PRO; PR:Q9P0K1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000008277; Expressed in 169 organ(s), highest expression level in cerebellum.
DR   ExpressionAtlas; Q9P0K1; baseline and differential.
DR   Genevisible; Q9P0K1; HS.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
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:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; NAS:UniProtKB.
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; IPR013032; EGF-like_CS.
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;
KW   Complete proteome; Disease mutation; Disulfide bond; EGF-like domain;
KW   Epilepsy; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
KW   Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   PROPEP       26    222       {ECO:0000250}.
FT                                /FTId=PRO_0000029112.
FT   CHAIN       223    906       Disintegrin and metalloproteinase domain-
FT                                containing protein 22.
FT                                /FTId=PRO_0000029113.
FT   TOPO_DOM    223    736       Extracellular. {ECO:0000255}.
FT   TRANSMEM    737    757       Helical. {ECO:0000255}.
FT   TOPO_DOM    758    906       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      239    438       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      444    531       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      675    712       EGF-like.
FT   COMPBIAS    532    678       Cys-rich.
FT   MOD_RES     810    810       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1V6}.
FT   MOD_RES     834    834       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     857    857       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1V6}.
FT   MOD_RES     862    862       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1V6}.
FT   MOD_RES     866    866       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1V6}.
FT   MOD_RES     870    870       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1V6}.
FT   CARBOHYD    175    175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    519    519       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19692335}.
FT   CARBOHYD    634    634       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19692335}.
FT   CARBOHYD    675    675       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19692335}.
FT   DISULFID    349    433       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    392    417       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    394    401       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    447    477       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    458    474       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    460    466       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    473    494       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    485    491       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    490    516       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    503    523       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    510    542       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    535    547       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    554    605       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    569    635       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    583    593       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    600    663       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    657    668       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    679    694       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    688    700       {ECO:0000269|PubMed:19692335}.
FT   DISULFID    702    711       {ECO:0000269|PubMed:19692335}.
FT   VAR_SEQ     768    803       Missing (in isoform 2, isoform 4 and
FT                                isoform 5). {ECO:0000303|PubMed:11050470,
FT                                ECO:0000303|PubMed:9693107,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_005482.
FT   VAR_SEQ     859    859       E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:11050470}.
FT                                /FTId=VSP_005484.
FT   VAR_SEQ     860    906       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000303|PubMed:9693107}.
FT                                /FTId=VSP_005483.
FT   VARIANT      81     81       P -> R (in dbSNP:rs2279542).
FT                                {ECO:0000269|PubMed:10524237,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_020057.
FT   VARIANT     119    119       H -> Y (in dbSNP:rs4728730).
FT                                /FTId=VAR_051589.
FT   VARIANT     207    207       V -> I (in dbSNP:rs17255978).
FT                                /FTId=VAR_051590.
FT   VARIANT     401    401       C -> Y (in EIEE61; unknown pathological
FT                                significance; loss of interaction with
FT                                LGI1; no effect on DLG4-binding, nor on
FT                                subcellular location; dbSNP:rs747259064).
FT                                {ECO:0000269|PubMed:27066583}.
FT                                /FTId=VAR_080496.
FT   MUTAGEN     834    834       S->A: Abolishes interactions with YWHAB
FT                                and YWHAZ; when associated with A-857.
FT                                {ECO:0000269|PubMed:12589811,
FT                                ECO:0000269|PubMed:15882968}.
FT   MUTAGEN     857    857       S->A: Abolishes interactions with YWHAB
FT                                and YWHAZ; when associated with A-834.
FT                                {ECO:0000269|PubMed:12589811,
FT                                ECO:0000269|PubMed:15882968}.
FT   STRAND      235    237       {ECO:0000244|PDB:3G5C}.
FT   STRAND      239    247       {ECO:0000244|PDB:3G5C}.
FT   HELIX       249    253       {ECO:0000244|PDB:3G5C}.
FT   TURN        254    257       {ECO:0000244|PDB:3G5C}.
FT   HELIX       259    280       {ECO:0000244|PDB:3G5C}.
FT   STRAND      281    292       {ECO:0000244|PDB:3G5C}.
FT   HELIX       305    318       {ECO:0000244|PDB:3G5C}.
FT   STRAND      325    333       {ECO:0000244|PDB:3G5C}.
FT   STRAND      336    338       {ECO:0000244|PDB:3G5C}.
FT   STRAND      341    343       {ECO:0000244|PDB:3G5C}.
FT   TURN        351    353       {ECO:0000244|PDB:3G5C}.
FT   STRAND      354    359       {ECO:0000244|PDB:3G5C}.
FT   HELIX       363    378       {ECO:0000244|PDB:3G5C}.
FT   HELIX       384    389       {ECO:0000244|PDB:3G5C}.
FT   STRAND      397    399       {ECO:0000244|PDB:5Y2Z}.
FT   HELIX       416    427       {ECO:0000244|PDB:3G5C}.
FT   HELIX       432    435       {ECO:0000244|PDB:3G5C}.
FT   HELIX       463    466       {ECO:0000244|PDB:3G5C}.
FT   TURN        467    473       {ECO:0000244|PDB:3G5C}.
FT   STRAND      474    479       {ECO:0000244|PDB:5Y2Z}.
FT   STRAND      486    488       {ECO:0000244|PDB:3G5C}.
FT   STRAND      491    496       {ECO:0000244|PDB:3G5C}.
FT   STRAND      502    504       {ECO:0000244|PDB:3G5C}.
FT   TURN        536    539       {ECO:0000244|PDB:3G5C}.
FT   STRAND      540    543       {ECO:0000244|PDB:3G5C}.
FT   STRAND      546    548       {ECO:0000244|PDB:3G5C}.
FT   HELIX       550    558       {ECO:0000244|PDB:3G5C}.
FT   HELIX       567    573       {ECO:0000244|PDB:3G5C}.
FT   TURN        574    576       {ECO:0000244|PDB:3G5C}.
FT   STRAND      585    590       {ECO:0000244|PDB:3G5C}.
FT   HELIX       595    597       {ECO:0000244|PDB:3G5C}.
FT   STRAND      600    602       {ECO:0000244|PDB:3G5C}.
FT   STRAND      605    607       {ECO:0000244|PDB:3G5C}.
FT   STRAND      613    617       {ECO:0000244|PDB:3G5C}.
FT   STRAND      622    628       {ECO:0000244|PDB:3G5C}.
FT   STRAND      631    637       {ECO:0000244|PDB:3G5C}.
FT   STRAND      640    645       {ECO:0000244|PDB:3G5C}.
FT   STRAND      656    658       {ECO:0000244|PDB:3G5C}.
FT   STRAND      661    666       {ECO:0000244|PDB:3G5C}.
FT   STRAND      668    670       {ECO:0000244|PDB:3G5C}.
FT   HELIX       671    674       {ECO:0000244|PDB:3G5C}.
FT   HELIX       688    690       {ECO:0000244|PDB:3G5C}.
FT   STRAND      692    695       {ECO:0000244|PDB:3G5C}.
FT   STRAND      700    702       {ECO:0000244|PDB:3G5C}.
FT   STRAND      706    708       {ECO:0000244|PDB:3G5C}.
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
//
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