ID   ADA22_MOUSE             Reviewed;         904 AA.
AC   Q9R1V6; Q5TLI8; Q5TLI9; Q5TLJ0; Q5TLJ1; Q5TLJ2; Q5TLJ3; Q5TLJ4; Q5TLJ5;
AC   Q5TLJ6; Q5TLJ7; Q5TLJ8; Q5TLJ9; Q5TLK0; Q5TLK1; Q5TLK2; Q5TLK3; Q5TLK4;
AC   Q5TLK5; Q5TLK6; Q5TLK7; Q5TLK8; Q8BSF2; Q9R1V5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   24-JAN-2024, entry version 187.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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; 8; 9;
RP   10; 11; 12; 13; 14; 15; 16; 17; 18; 19; 20 AND 21), TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15876356; DOI=10.1186/1471-2202-6-33;
RA   Sagane K., Hayakawa K., Kai J., Hirohashi T., Takahashi E., Miyamoto N.,
RA   Ino M., Oki T., Yamazaki K., Nagasu T.;
RT   "Ataxia and peripheral nerve hypomyelination in ADAM22-deficient 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 synaptic
RT   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] AT
RP   SER-882 (ISOFORM 12), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817
RP   (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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 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., Burlingame A.L.,
RA   Trimmer J.S., Meijer D., Rasband M.N.;
RT   "ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated
RT   guanylate kinases to juxtaparanodes of myelinated axons.";
RL   J. Neurosci. 30:1038-1048(2010).
RN   [8]
RP   INTERACTION WITH ADAM11, AND TISSUE SPECIFICITY.
RX   PubMed=26269648; DOI=10.1523/jneurosci.1346-15.2015;
RA   Kole M.J., Qian J., Waase M.P., Klassen T.L., Chen T.T., Augustine G.J.,
RA   Noebels J.L.;
RT   "Selective Loss of Presynaptic Potassium Channel Clusters at the Cerebellar
RT   Basket Cell Terminal Pinceau in Adam11 Mutants Reveals Their Role in
RT   Ephaptic Control of Purkinje Cell Firing.";
RL   J. Neurosci. 35:11433-11444(2015).
CC   -!- FUNCTION: Probable ligand for integrin in the brain. This is a non
CC       catalytic metalloprotease-like protein. Involved in regulation of cell
CC       adhesion and spreading and in inhibition of cell proliferation (By
CC       similarity). Neuronal receptor for LGI1. {ECO:0000250|UniProtKB:Q9P0K1,
CC       ECO:0000269|PubMed:16990550}.
CC   -!- SUBUNIT: Interacts with LGI1 (PubMed:16990550, PubMed:18974846,
CC       PubMed:20089912). Can bind to LGI4 (PubMed:18974846). Interacts with
CC       KCNA2, DLG2 and DLG4 (PubMed:20089912). Interacts with ADAM11
CC       (PubMed:26269648). Interacts (via C-terminus) with YWHAB/14-3-3 beta
CC       (By similarity). Interacts (via C-terminus) with YWHAZ/14-3-3 zeta (By
CC       similarity). {ECO:0000250|UniProtKB:Q9P0K1,
CC       ECO:0000269|PubMed:16990550, ECO:0000269|PubMed:18974846,
CC       ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:26269648}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20089912};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC       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       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       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 central
CC       nervous system and at nerve terminal plexuses of basket cells in the
CC       cerebellum (at protein level) (PubMed:20089912, PubMed:26269648).
CC       Expressed at high levels in the brain. Strongly expressed in cerebellar
CC       granule cells and hippocampus. In spinal cord, expression is restricted
CC       to gray matter. {ECO:0000269|PubMed:15876356,
CC       ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:26269648}.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice display severe ataxia within one week after
CC       birth and die before weaning, probably due to convulsions. They display
CC       marked hypomyelination of the peripheral nerves.
CC       {ECO:0000269|PubMed:15876356}.
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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.
DR   PDB; 7EXE; X-ray; 2.75 A; C=827-857.
DR   PDBsum; 7EXE; -.
DR   AlphaFoldDB; Q9R1V6; -.
DR   SMR; Q9R1V6; -.
DR   BioGRID; 197967; 24.
DR   IntAct; Q9R1V6; 5.
DR   STRING; 10090.ENSMUSP00000086139; -.
DR   MEROPS; M12.978; -.
DR   GlyConnect; 2258; 1 N-Linked glycan (1 site).
DR   GlyConnect; 2413; 11 N-Linked glycans (3 sites). [Q9R1V6-16]
DR   GlyConnect; 2443; 6 N-Linked glycans (2 sites). [Q9R1V6-10]
DR   GlyConnect; 2444; 2 N-Linked glycans (2 sites). [Q9R1V6-11]
DR   GlyCosmos; Q9R1V6; 5 sites, 14 glycans.
DR   GlyGen; Q9R1V6; 6 sites, 14 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9R1V6; -.
DR   PhosphoSitePlus; Q9R1V6; -.
DR   SwissPalm; Q9R1V6; -.
DR   MaxQB; Q9R1V6; -.
DR   PaxDb; 10090-ENSMUSP00000055000; -.
DR   PeptideAtlas; Q9R1V6; -.
DR   ProteomicsDB; 285860; -. [Q9R1V6-3]
DR   ProteomicsDB; 285861; -. [Q9R1V6-4]
DR   ProteomicsDB; 285862; -. [Q9R1V6-5]
DR   ProteomicsDB; 285863; -. [Q9R1V6-6]
DR   ProteomicsDB; 285864; -. [Q9R1V6-7]
DR   ProteomicsDB; 285865; -. [Q9R1V6-8]
DR   ProteomicsDB; 285866; -. [Q9R1V6-9]
DR   ProteomicsDB; 285867; -. [Q9R1V6-10]
DR   ProteomicsDB; 285868; -. [Q9R1V6-11]
DR   ProteomicsDB; 285869; -. [Q9R1V6-12]
DR   ProteomicsDB; 285870; -. [Q9R1V6-13]
DR   ProteomicsDB; 285871; -. [Q9R1V6-14]
DR   ProteomicsDB; 285872; -. [Q9R1V6-15]
DR   ProteomicsDB; 285873; -. [Q9R1V6-16]
DR   ProteomicsDB; 285874; -. [Q9R1V6-17]
DR   ProteomicsDB; 285875; -. [Q9R1V6-18]
DR   ProteomicsDB; 285876; -. [Q9R1V6-2]
DR   ProteomicsDB; 285877; -. [Q9R1V6-19]
DR   ProteomicsDB; 285878; -. [Q9R1V6-20]
DR   ProteomicsDB; 285879; -. [Q9R1V6-1]
DR   ProteomicsDB; 285880; -. [Q9R1V6-21]
DR   ABCD; Q9R1V6; 2 sequenced antibodies.
DR   Antibodypedia; 29782; 354 antibodies from 26 providers.
DR   DNASU; 11496; -.
DR   Ensembl; ENSMUST00000046838.14; ENSMUSP00000049120.8; ENSMUSG00000040537.18. [Q9R1V6-1]
DR   Ensembl; ENSMUST00000050166.14; ENSMUSP00000055000.8; ENSMUSG00000040537.18. [Q9R1V6-4]
DR   Ensembl; ENSMUST00000088744.12; ENSMUSP00000086122.6; ENSMUSG00000040537.18. [Q9R1V6-13]
DR   Ensembl; ENSMUST00000088761.11; ENSMUSP00000086139.5; ENSMUSG00000040537.18. [Q9R1V6-3]
DR   Ensembl; ENSMUST00000115388.9; ENSMUSP00000111046.3; ENSMUSG00000040537.18. [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   AGR; MGI:1340046; -.
DR   CTD; 53616; -.
DR   MGI; MGI:1340046; Adam22.
DR   VEuPathDB; HostDB:ENSMUSG00000040537; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000156889; -.
DR   HOGENOM; CLU_012714_5_2_1; -.
DR   InParanoid; Q9R1V6; -.
DR   OMA; TAWGYNM; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q9R1V6; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   BioGRID-ORCS; 11496; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Adam22; mouse.
DR   PRO; PR:Q9R1V6; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9R1V6; Protein.
DR   Bgee; ENSMUSG00000040537; Expressed in cerebellum lobe and 194 other cell types or tissues.
DR   ExpressionAtlas; Q9R1V6; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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; IDA:SynGO.
DR   GO; GO:1903829; P:positive regulation of protein localization; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
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   PROSITE; PS50026; EGF_3; 1.
DR   Genevisible; Q9R1V6; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..223
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029114"
FT   CHAIN           224..904
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 22"
FT                   /id="PRO_0000029115"
FT   TOPO_DOM        24..734
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        735..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        756..857
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          237..436
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          442..529
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          673..710
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          769..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         808
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         832
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         864
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         868
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        347..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        390..415
FT                   /evidence="ECO:0000250"
FT   DISULFID        392..399
FT                   /evidence="ECO:0000250"
FT   DISULFID        445..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        456..472
FT                   /evidence="ECO:0000250"
FT   DISULFID        458..464
FT                   /evidence="ECO:0000250"
FT   DISULFID        471..492
FT                   /evidence="ECO:0000250"
FT   DISULFID        483..489
FT                   /evidence="ECO:0000250"
FT   DISULFID        488..514
FT                   /evidence="ECO:0000250"
FT   DISULFID        501..521
FT                   /evidence="ECO:0000250"
FT   DISULFID        508..540
FT                   /evidence="ECO:0000250"
FT   DISULFID        533..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        552..603
FT                   /evidence="ECO:0000250"
FT   DISULFID        567..633
FT                   /evidence="ECO:0000250"
FT   DISULFID        581..591
FT                   /evidence="ECO:0000250"
FT   DISULFID        598..661
FT                   /evidence="ECO:0000250"
FT   DISULFID        655..666
FT                   /evidence="ECO:0000250"
FT   DISULFID        677..692
FT                   /evidence="ECO:0000250"
FT   DISULFID        686..698
FT                   /evidence="ECO:0000250"
FT   DISULFID        700..709
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         730..904
FT                   /note="VAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDS
FT                   FYSDFPPGGSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGN
FT                   KKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSARL
FT                   WETSI -> QMDSLILGVKGFQTQNIFQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDL
FT                   DLTQLRPCHLPSLLLHQLGLLPPAENTRTLCLRFQTRGRQRADRAPGYGRHPF (in
FT                   isoform 16)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018233"
FT   VAR_SEQ         760..904
FT                   /note="NYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSE
FT                   RIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTG
FT                   SIASSRKYPYPMPPLPDEGKTAGRQSARLWETSI -> FPPVPSHIIPLVRTFHYFAAG
FT                   QMDSLILGVKGFQTQNIFQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDLDLTQLRPCH
FT                   LPSLLLHQLGLLPPAENTRTLCLRFQTRGRQRADRAPGYGRHPF (in isoform
FT                   14)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018234"
FT   VAR_SEQ         760..801
FT                   /note="Missing (in isoform 3, isoform 4 and isoform 18)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018235"
FT   VAR_SEQ         760..765
FT                   /note="Missing (in isoform 11 and isoform 19)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018236"
FT   VAR_SEQ         766..846
FT                   /note="QLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSERIPDTK
FT                   HISDICENGRPRSNSWQGNMGGNKKKIRG -> FPPVPSHIIPLVRTFHYFAAGQMDSL
FT                   ILGVKGFQTQNIFQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDLDLTQLSKLYL (in
FT                   isoform 21)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018237"
FT   VAR_SEQ         766..801
FT                   /note="Missing (in isoform 2, isoform 5, isoform 8, isoform
FT                   15 and isoform 17)"
FT                   /evidence="ECO:0000303|PubMed:10433968,
FT                   ECO:0000303|PubMed:15876356, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018238"
FT   VAR_SEQ         802
FT                   /note="S -> SAFLSHFQISTCSITHYSISQNISLFCSRS (in isoform 10,
FT                   isoform 11, isoform 12 and isoform 13)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018239"
FT   VAR_SEQ         847..904
FT                   /note="Missing (in isoform 21)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018240"
FT   VAR_SEQ         857..904
FT                   /note="ETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSARLWETSI ->
FT                   DLGIIT (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018241"
FT   VAR_SEQ         857
FT                   /note="E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLDHSSQDGPHQQD
FT                   R (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018242"
FT   VAR_SEQ         857
FT                   /note="E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in isoform 12)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018243"
FT   VAR_SEQ         857
FT                   /note="E -> DSQDGPHQQDR (in isoform 15)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018244"
FT   VAR_SEQ         857
FT                   /note="E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLDHR (in
FT                   isoform 4, isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018245"
FT   VAR_SEQ         857
FT                   /note="E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFSSQDSPHQQDR (in
FT                   isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018246"
FT   VAR_SEQ         857
FT                   /note="E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLDHRYLNPWFKRD
FT                   YNVAKWVEDVNKNTEGPYFR (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018247"
FT   VAR_SEQ         858..904
FT                   /note="Missing (in isoform 17, isoform 18, isoform 19 and
FT                   isoform 20)"
FT                   /evidence="ECO:0000303|PubMed:10433968,
FT                   ECO:0000303|PubMed:15876356"
FT                   /id="VSP_018248"
FT   MUTAGEN         509
FT                   /note="D->N: Fails to bind to LGI1."
FT                   /evidence="ECO:0000269|PubMed:16990550"
FT   CONFLICT        639
FT                   /note="K -> R (in Ref. 2; BAC28742)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q9R1V6-10:817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9R1V6-14:882
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
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
//