ADA22_MOUSE
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 03-AUG-2022, entry version 179.
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).
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:18974846, PubMed:20089912). Can
CC bind to LGI4(PubMed:18974846). Interacts with KCNA2, DLG2 and DLG4
CC (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 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). Expressed at high
CC levels in the brain. Strongly expressed in cerebellar granule cells and
CC hippocampus. In spinal cord, 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. {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. [Q9R1V6-5]
DR PDB; 7EXE; X-ray; 2.75 A; C=827-857.
DR PDBsum; 7EXE; -.
DR AlphaFoldDB; Q9R1V6; -.
DR SMR; Q9R1V6; -.
DR BioGRID; 197967; 22.
DR IntAct; Q9R1V6; 5.
DR STRING; 10090.ENSMUSP00000055000; -.
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 GlyGen; Q9R1V6; 5 sites, 14 N-linked glycans (4 sites).
DR iPTMnet; Q9R1V6; -.
DR PhosphoSitePlus; Q9R1V6; -.
DR MaxQB; Q9R1V6; -.
DR PaxDb; Q9R1V6; -.
DR PeptideAtlas; Q9R1V6; -.
DR PRIDE; 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; 343 antibodies from 26 providers.
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 VEuPathDB; HostDB:ENSMUSG00000040537; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156889; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR InParanoid; Q9R1V6; -.
DR OMA; TAWGYKK; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R1V6; -.
DR TreeFam; TF314733; -.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR BioGRID-ORCS; 11496; 0 hits in 71 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 193 other tissues.
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; IMP:SynGO.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 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 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
