GenomeNet

Database: UniProt
Entry: Q9R1V6
LinkDB: Q9R1V6
Original site: Q9R1V6 
ID   ADA22_MOUSE             Reviewed;         904 AA.
AC   Q9R1V6; Q5TLI8; Q5TLI9; Q5TLJ0; Q5TLJ1; Q5TLJ2; Q5TLJ3; Q5TLJ4;
AC   Q5TLJ5; Q5TLJ6; Q5TLJ7; Q5TLJ8; Q5TLJ9; Q5TLK0; Q5TLK1; Q5TLK2;
AC   Q5TLK3; Q5TLK4; Q5TLK5; Q5TLK6; Q5TLK7; Q5TLK8; Q8BSF2; Q9R1V5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   13-FEB-2019, entry version 159.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22;
DE            Short=ADAM 22;
DE   Flags: Precursor;
GN   Name=Adam22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 17 AND 20).
RC   TISSUE=Brain;
RX   PubMed=10433968; DOI=10.1016/S0378-1119(99)00253-X;
RA   Sagane K., Yamazaki K., Mizui Y., Tanaka I.;
RT   "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23.";
RL   Gene 236:79-86(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-904 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 709-904 (ISOFORMS 1; 2; 3; 4; 5; 6; 7;
RP   8; 9; 10; 11; 12; 13; 14; 15; 16; 17; 18; 19; 20 AND 21), TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15876356; DOI=10.1186/1471-2202-6-33;
RA   Sagane K., Hayakawa K., Kai J., Hirohashi T., Takahashi E.,
RA   Miyamoto N., Ino M., Oki T., Yamazaki K., Nagasu T.;
RT   "Ataxia and peripheral nerve hypomyelination in ADAM22-deficient
RT   mice.";
RL   BMC Neurosci. 6:33-33(2005).
RN   [4]
RP   FUNCTION, INTERACTION WITH LGI1, AND MUTAGENESIS OF ASP-509.
RX   PubMed=16990550; DOI=10.1126/science.1129947;
RA   Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.;
RT   "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate
RT   synaptic transmission.";
RL   Science 313:1792-1795(2006).
RN   [5]
RP   INTERACTION WITH LIGI1 AND LGI4.
RX   PubMed=18974846; DOI=10.7150/ijbs.4.387;
RA   Sagane K., Ishihama Y., Sugimoto H.;
RT   "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11.";
RL   Int. J. Biol. Sci. 4:387-396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808; SER-832; SER-855;
RP   SER-860; SER-864 AND SER-868, PHOSPHORYLATION [LARGE SCALE ANALYSIS]
RP   AT SER-882 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-817 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INTERACTION WITH KCNA2; LGI1; DLG2 AND DLG4, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=20089912; DOI=10.1523/JNEUROSCI.4661-09.2010;
RA   Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E.,
RA   Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.;
RT   "ADAM22, a Kv1 channel-interacting protein, recruits membrane-
RT   associated guanylate kinases to juxtaparanodes of myelinated axons.";
RL   J. Neurosci. 30:1038-1048(2010).
CC   -!- FUNCTION: Probable ligand for integrin in the brain. This is a non
CC       catalytic metalloprotease-like protein. Involved in regulation of
CC       cell adhesion and spreading and in inhibition of cell
CC       proliferation (By similarity). Neuronal receptor for LGI1.
CC       {ECO:0000250|UniProtKB:Q9P0K1, ECO:0000269|PubMed:16990550}.
CC   -!- SUBUNIT: Interacts with LGI1 (PubMed:18974846, PubMed:20089912).
CC       Can bind to LGI4(PubMed:18974846). Interacts with KCNA2, DLG2 and
CC       DLG4 (PubMed:20089912). {ECO:0000269|PubMed:16990550,
CC       ECO:0000269|PubMed:18974846, ECO:0000269|PubMed:20089912}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20089912};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell
CC       projection, axon {ECO:0000269|PubMed:20089912}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=21;
CC       Name=1; Synonyms=ADAM22-G01, 22g;
CC         IsoId=Q9R1V6-3; Sequence=Displayed;
CC       Name=2; Synonyms=ADAM22-G03, 22g(D27);
CC         IsoId=Q9R1V6-4; Sequence=VSP_018238;
CC       Name=3; Synonyms=ADAM22-G06, 22g(D26D27);
CC         IsoId=Q9R1V6-5; Sequence=VSP_018235;
CC       Name=4; Synonyms=ADAM22=G07, 22g(D26D27)+29.3;
CC         IsoId=Q9R1V6-6; Sequence=VSP_018235, VSP_018245;
CC       Name=5; Synonyms=ADAM22-G08, 22g(D27)+29.3;
CC         IsoId=Q9R1V6-7; Sequence=VSP_018238, VSP_018245;
CC       Name=6; Synonyms=ADAM22-G09, 22g+29.3;
CC         IsoId=Q9R1V6-8; Sequence=VSP_018245;
CC       Name=7; Synonyms=ADAM22-G10, 22g+29.1;
CC         IsoId=Q9R1V6-9; Sequence=VSP_018241;
CC       Name=8; Synonyms=ADAM22-G11, 22g(D27)+29.5+29.7;
CC         IsoId=Q9R1V6-10; Sequence=VSP_018238, VSP_018246;
CC         Note=Contains a phosphoserine at position 817.
CC         {ECO:0000244|PubMed:21183079};
CC       Name=9; Synonyms=ADAM22-G12, 22g+29.3+29.7;
CC         IsoId=Q9R1V6-11; Sequence=VSP_018247;
CC       Name=10; Synonyms=ADAM22-G17, 22G[27L]+29.3+29.7;
CC         IsoId=Q9R1V6-12; Sequence=VSP_018239, VSP_018242;
CC       Name=11; Synonyms=ADAM22-G18, 22g(D26)[27L];
CC         IsoId=Q9R1V6-13; Sequence=VSP_018236, VSP_018239;
CC       Name=12; Synonyms=ADAM22-G19, 22g[27L]+29.5;
CC         IsoId=Q9R1V6-14; Sequence=VSP_018239, VSP_018243;
CC         Note=Contains a phosphoserine at position 882.
CC         {ECO:0000244|PubMed:21183079};
CC       Name=13; Synonyms=ADAM22-G20, 22g[27L];
CC         IsoId=Q9R1V6-15; Sequence=VSP_018239;
CC       Name=14; Synonyms=ADAM22-G21, 22g(D26)[27S];
CC         IsoId=Q9R1V6-16; Sequence=VSP_018234;
CC       Name=15; Synonyms=ADAM22-G22, 22g(D27)+29.7;
CC         IsoId=Q9R1V6-17; Sequence=VSP_018238, VSP_018244;
CC       Name=16; Synonyms=ADAM22-G23, 22g(D25D26D27);
CC         IsoId=Q9R1V6-18; Sequence=VSP_018233;
CC       Name=17; Synonyms=ADAM22-A05, Beta;
CC         IsoId=Q9R1V6-2; Sequence=VSP_018238, VSP_018248;
CC       Name=18; Synonyms=ADAM22-A13;
CC         IsoId=Q9R1V6-19; Sequence=VSP_018235, VSP_018248;
CC       Name=19; Synonyms=ADAM22-A15;
CC         IsoId=Q9R1V6-20; Sequence=VSP_018236, VSP_018248;
CC       Name=20; Synonyms=ADAM22-A04, Alpha;
CC         IsoId=Q9R1V6-1; Sequence=VSP_018248;
CC       Name=21; Synonyms=ADAM22-A16;
CC         IsoId=Q9R1V6-21; Sequence=VSP_018237, VSP_018240;
CC   -!- TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the
CC       central nervous system and at nerve terminal plexuses of basket
CC       cells in the cerebellum (at protein level) (PubMed:20089912).
CC       Expressed at high levels in the brain. Strongly expressed in
CC       cerebellar granule cells and hippocampus. In spinal cord,
CC       expression is restricted to gray matter.
CC       {ECO:0000269|PubMed:15876356, ECO:0000269|PubMed:20089912}.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice display severe ataxia within one week
CC       after birth and die before weaning, probably due to convulsions.
CC       They display marked hypomyelination of the peripheral nerves.
CC       {ECO:0000269|PubMed:15876356}.
DR   EMBL; AB009674; BAA83382.1; -; mRNA.
DR   EMBL; AB009674; BAA83383.1; -; mRNA.
DR   EMBL; AK034528; BAC28742.1; -; mRNA.
DR   EMBL; AB179842; BAD72803.1; -; mRNA.
DR   EMBL; AB179843; BAD72804.1; -; mRNA.
DR   EMBL; AB179844; BAD72805.1; -; mRNA.
DR   EMBL; AB179845; BAD72806.1; -; mRNA.
DR   EMBL; AB179846; BAD72807.1; -; mRNA.
DR   EMBL; AB179847; BAD72808.1; -; mRNA.
DR   EMBL; AB179848; BAD72809.1; -; mRNA.
DR   EMBL; AB179849; BAD72810.1; -; mRNA.
DR   EMBL; AB179850; BAD72811.1; -; mRNA.
DR   EMBL; AB179851; BAD72812.1; -; mRNA.
DR   EMBL; AB179852; BAD72813.1; -; mRNA.
DR   EMBL; AB179853; BAD72814.1; -; mRNA.
DR   EMBL; AB179854; BAD72815.1; -; mRNA.
DR   EMBL; AB179855; BAD72816.1; -; mRNA.
DR   EMBL; AB179856; BAD72817.1; -; mRNA.
DR   EMBL; AB179857; BAD72818.1; -; mRNA.
DR   EMBL; AB179858; BAD72819.1; -; mRNA.
DR   EMBL; AB179859; BAD72820.1; -; mRNA.
DR   EMBL; AB179860; BAD72821.1; -; mRNA.
DR   EMBL; AB179861; BAD72822.1; -; mRNA.
DR   EMBL; AB179862; BAD72823.1; -; mRNA.
DR   CCDS; CCDS19080.1; -. [Q9R1V6-1]
DR   CCDS; CCDS51411.1; -. [Q9R1V6-4]
DR   CCDS; CCDS80205.1; -. [Q9R1V6-6]
DR   CCDS; CCDS80207.1; -. [Q9R1V6-3]
DR   RefSeq; NP_001007221.1; NM_001007220.3. [Q9R1V6-1]
DR   RefSeq; NP_001007222.1; NM_001007221.3. [Q9R1V6-2]
DR   RefSeq; NP_001091695.1; NM_001098225.2. [Q9R1V6-4]
DR   RefSeq; NP_001297368.1; NM_001310439.1. [Q9R1V6-6]
DR   RefSeq; NP_001297369.1; NM_001310440.1. [Q9R1V6-3]
DR   RefSeq; XP_006503592.1; XM_006503529.3. [Q9R1V6-12]
DR   RefSeq; XP_006503593.1; XM_006503530.3. [Q9R1V6-11]
DR   RefSeq; XP_006503594.1; XM_006503531.3. [Q9R1V6-14]
DR   RefSeq; XP_006503596.1; XM_006503533.3. [Q9R1V6-8]
DR   RefSeq; XP_006503598.1; XM_006503535.3. [Q9R1V6-15]
DR   RefSeq; XP_006503600.1; XM_006503537.3. [Q9R1V6-7]
DR   RefSeq; XP_006503605.1; XM_006503542.3. [Q9R1V6-5]
DR   UniGene; Mm.275895; -.
DR   ProteinModelPortal; Q9R1V6; -.
DR   SMR; Q9R1V6; -.
DR   BioGrid; 197967; 4.
DR   IntAct; Q9R1V6; 8.
DR   MINT; Q9R1V6; -.
DR   STRING; 10090.ENSMUSP00000055000; -.
DR   MEROPS; M12.978; -.
DR   iPTMnet; Q9R1V6; -.
DR   PhosphoSitePlus; Q9R1V6; -.
DR   MaxQB; Q9R1V6; -.
DR   PaxDb; Q9R1V6; -.
DR   PeptideAtlas; Q9R1V6; -.
DR   PRIDE; Q9R1V6; -.
DR   DNASU; 11496; -.
DR   Ensembl; ENSMUST00000046838; ENSMUSP00000049120; ENSMUSG00000040537. [Q9R1V6-1]
DR   Ensembl; ENSMUST00000050166; ENSMUSP00000055000; ENSMUSG00000040537. [Q9R1V6-4]
DR   Ensembl; ENSMUST00000088744; ENSMUSP00000086122; ENSMUSG00000040537. [Q9R1V6-13]
DR   Ensembl; ENSMUST00000088761; ENSMUSP00000086139; ENSMUSG00000040537. [Q9R1V6-3]
DR   Ensembl; ENSMUST00000115388; ENSMUSP00000111046; ENSMUSG00000040537. [Q9R1V6-6]
DR   GeneID; 11496; -.
DR   KEGG; mmu:11496; -.
DR   UCSC; uc008wjk.2; mouse. [Q9R1V6-3]
DR   UCSC; uc008wjv.1; mouse. [Q9R1V6-4]
DR   UCSC; uc008wjy.1; mouse. [Q9R1V6-2]
DR   CTD; 53616; -.
DR   MGI; MGI:1340046; Adam22.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000156889; -.
DR   HOVERGEN; HBG050456; -.
DR   InParanoid; Q9R1V6; -.
DR   KO; K16068; -.
DR   OMA; SWQGNIG; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9R1V6; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   ChiTaRS; Adam22; mouse.
DR   PRO; PR:Q9R1V6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000040537; Expressed in 217 organ(s), highest expression level in brain.
DR   ExpressionAtlas; Q9R1V6; baseline and differential.
DR   Genevisible; Q9R1V6; MM.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0042063; P:gliogenesis; IGI:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; EXP:SynGO.
DR   GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
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; 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.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   PROPEP       24    223       {ECO:0000250}.
FT                                /FTId=PRO_0000029114.
FT   CHAIN       224    904       Disintegrin and metalloproteinase domain-
FT                                containing protein 22.
FT                                /FTId=PRO_0000029115.
FT   TOPO_DOM     24    734       Extracellular. {ECO:0000255}.
FT   TRANSMEM    735    755       Helical. {ECO:0000255}.
FT   TOPO_DOM    756    857       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      237    436       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      442    529       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      673    710       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    533    666       Cys-rich.
FT   MOD_RES     808    808       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     832    832       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     855    855       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     860    860       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     864    864       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     868    868       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    517    517       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    632    632       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    673    673       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    347    431       {ECO:0000250}.
FT   DISULFID    390    415       {ECO:0000250}.
FT   DISULFID    392    399       {ECO:0000250}.
FT   DISULFID    445    475       {ECO:0000250}.
FT   DISULFID    456    472       {ECO:0000250}.
FT   DISULFID    458    464       {ECO:0000250}.
FT   DISULFID    471    492       {ECO:0000250}.
FT   DISULFID    483    489       {ECO:0000250}.
FT   DISULFID    488    514       {ECO:0000250}.
FT   DISULFID    501    521       {ECO:0000250}.
FT   DISULFID    508    540       {ECO:0000250}.
FT   DISULFID    533    545       {ECO:0000250}.
FT   DISULFID    552    603       {ECO:0000250}.
FT   DISULFID    567    633       {ECO:0000250}.
FT   DISULFID    581    591       {ECO:0000250}.
FT   DISULFID    598    661       {ECO:0000250}.
FT   DISULFID    655    666       {ECO:0000250}.
FT   DISULFID    677    692       {ECO:0000250}.
FT   DISULFID    686    698       {ECO:0000250}.
FT   DISULFID    700    709       {ECO:0000250}.
FT   VAR_SEQ     730    904       VAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQG
FT                                DYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSE
FT                                RIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPR
FT                                SNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAG
FT                                RQSARLWETSI -> QMDSLILGVKGFQTQNIFQTSVKMGD
FT                                LAVTPGKVTWEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQ
FT                                LGLLPPAENTRTLCLRFQTRGRQRADRAPGYGRHPF (in
FT                                isoform 16).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018233.
FT   VAR_SEQ     760    904       NYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKK
FT                                RSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGNK
FT                                KKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPM
FT                                PPLPDEGKTAGRQSARLWETSI -> FPPVPSHIIPLVRTF
FT                                HYFAAGQMDSLILGVKGFQTQNIFQTSVKMGDLAVTPGKVT
FT                                WEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQLGLLPPAEN
FT                                TRTLCLRFQTRGRQRADRAPGYGRHPF (in isoform
FT                                14). {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018234.
FT   VAR_SEQ     760    801       Missing (in isoform 3, isoform 4 and
FT                                isoform 18).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018235.
FT   VAR_SEQ     760    765       Missing (in isoform 11 and isoform 19).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018236.
FT   VAR_SEQ     766    846       QLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLS
FT                                HSWSERIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRG
FT                                -> FPPVPSHIIPLVRTFHYFAAGQMDSLILGVKGFQTQNI
FT                                FQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDLDLTQLSKL
FT                                YL (in isoform 21).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018237.
FT   VAR_SEQ     766    801       Missing (in isoform 2, isoform 5, isoform
FT                                8, isoform 15 and isoform 17).
FT                                {ECO:0000303|PubMed:10433968,
FT                                ECO:0000303|PubMed:15876356,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_018238.
FT   VAR_SEQ     802    802       S -> SAFLSHFQISTCSITHYSISQNISLFCSRS (in
FT                                isoform 10, isoform 11, isoform 12 and
FT                                isoform 13).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018239.
FT   VAR_SEQ     847    904       Missing (in isoform 21).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018240.
FT   VAR_SEQ     857    904       ETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSA
FT                                RLWETSI -> DLGIIT (in isoform 7).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018241.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HSSQDGPHQQDR (in isoform 10).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018242.
FT   VAR_SEQ     857    857       E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in
FT                                isoform 12).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018243.
FT   VAR_SEQ     857    857       E -> DSQDGPHQQDR (in isoform 15).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018244.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HR (in isoform 4, isoform 5 and isoform
FT                                6). {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018245.
FT   VAR_SEQ     857    857       E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFSSQDSPH
FT                                QQDR (in isoform 8).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018246.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HRYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in
FT                                isoform 9).
FT                                {ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018247.
FT   VAR_SEQ     858    904       Missing (in isoform 17, isoform 18,
FT                                isoform 19 and isoform 20).
FT                                {ECO:0000303|PubMed:10433968,
FT                                ECO:0000303|PubMed:15876356}.
FT                                /FTId=VSP_018248.
FT   MUTAGEN     509    509       D->N: Fails to bind to LGI1.
FT                                {ECO:0000269|PubMed:16990550}.
FT   CONFLICT    639    639       K -> R (in Ref. 2; BAC28742).
FT                                {ECO:0000305}.
SQ   SEQUENCE   904 AA;  99715 MW;  0FBBD09398EE0B97 CRC64;
     MQAAAAASFW LLCVLGTCPL ARCGRAGVAS LKGLERGKEN RFLERQSIIP LRLIYRLGGE
     DETQHNQLDT RVRGDPGGPQ LTHVDKASFR VDAFGTSFVL DVLLNHELLS SGYVERQIEH
     GGKVVENKGG EHCYYQGQIR GNPVSFVALS TCHGLHGMFY DGNHTYLIEP EENEKSQESS
     HCHSVYKSRQ FEFPLDDLPS EFQRVNITPP QFILKPRLKR RKRQLLRFPR NVEEETKYIE
     LMIVNDHLMF KKHRLSVVYT NTYAKSVVNM ADVIYKDQLK TRIVLVAMET WAADNKFAIS
     ENPLITLREF MKYRRDFIKE KADAVHLFSG SQFESSRSGA AYIGGICSLL RGGGVNEFGK
     TDLMAVTLAQ SLAHNVGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNVEEY
     HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECALEGAE CCKKCTLTQD
     SQCSDGLCCK KCKFQPLGTV CREAVNDCDI REICSGNSSQ CAPNVHKMDG YSCDGTQGIC
     FGGRCKTRDR QCKYIWGQKV TASDRYCYEK LNIEGTEKGN CGKDKDTWTQ CNKRDVLCGY
     LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGAHVKL EEDVDLGYVE DGTPCGPQMM
     CLEHRCLPVA SFNFSTCSSS KAGTVCSGNG VCSNELKCVC NRHWTGADCG THFPHNDDAK
     TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRQLPQG DYVKKPGDGD
     SFYSDFPPGG STNSASSSKK RSNGLSHSWS ERIPDTKHIS DICENGRPRS NSWQGNMGGN
     KKKIRGKRFR PRSNSTETLS PAKSPSSSTG SIASSRKYPY PMPPLPDEGK TAGRQSARLW
     ETSI
//
DBGET integrated database retrieval system