AMGO2_MOUSE
ID AMGO2_MOUSE Reviewed; 519 AA.
AC Q80ZD9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Amphoterin-induced protein 2;
DE AltName: Full=AMIGO-2;
DE AltName: Full=Alivin-1;
DE Flags: Precursor;
GN Name=Amigo2 {ECO:0000312|EMBL:AAO48947.1};
GN Synonyms=Ali1 {ECO:0000312|EMBL:BAC81187.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAO48947.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO48947.1};
RC TISSUE=Brain {ECO:0000269|PubMed:12629050};
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.;
RT "AMIGO, a transmembrane protein implicated in axon tract development,
RT defines a novel protein family with leucine-rich repeats.";
RL J. Cell Biol. 160:963-973(2003).
RN [2] {ECO:0000312|EMBL:BAC81187.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR {ECO:0000312|EMBL:BAC81187.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAC81187.1};
RX PubMed=12843293; DOI=10.1523/jneurosci.23-13-05887.2003;
RA Ono T., Sekino-Suzuki N., Kikkawa Y., Yonekawa H., Kawashima S.;
RT "Alivin 1, a novel neuronal activity-dependent gene, inhibits apoptosis and
RT promotes survival of cerebellar granule neurons.";
RL J. Neurosci. 23:5887-5896(2003).
CC -!- FUNCTION: Required for depolarization-dependent survival of cultured
CC cerebellar granule neurons. May mediate homophilic as well as
CC heterophilic cell-cell interaction with AMIGO1 or AMIGO3. May
CC contribute to signal transduction through its intracellular domain (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated
CC with nucleus as well as plasma membrane. Restricted to somata of
CC cerebellar as well as hippocampal neurons (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest level in cerebellum, retina, liver, and
CC lung. Lower levels in cerebrum, kidney, small intestine, spleen and
CC testis. {ECO:0000269|PubMed:12629050}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237006; AAO48947.1; -; mRNA.
DR EMBL; AB078880; BAC81187.1; -; mRNA.
DR CCDS; CCDS27780.1; -.
DR RefSeq; NP_001158035.1; NM_001164563.1.
DR RefSeq; NP_001158074.1; NM_001164602.1.
DR RefSeq; NP_835215.1; NM_178114.4.
DR AlphaFoldDB; Q80ZD9; -.
DR SMR; Q80ZD9; -.
DR STRING; 10090.ENSMUSP00000059913; -.
DR GlyGen; Q80ZD9; 9 sites.
DR iPTMnet; Q80ZD9; -.
DR PhosphoSitePlus; Q80ZD9; -.
DR MaxQB; Q80ZD9; -.
DR PaxDb; Q80ZD9; -.
DR PRIDE; Q80ZD9; -.
DR ProteomicsDB; 296027; -.
DR Antibodypedia; 13397; 242 antibodies from 31 providers.
DR DNASU; 105827; -.
DR Ensembl; ENSMUST00000053106; ENSMUSP00000059913; ENSMUSG00000048218.
DR Ensembl; ENSMUST00000229890; ENSMUSP00000155019; ENSMUSG00000048218.
DR GeneID; 105827; -.
DR KEGG; mmu:105827; -.
DR UCSC; uc007xks.2; mouse.
DR CTD; 347902; -.
DR MGI; MGI:2145995; Amigo2.
DR VEuPathDB; HostDB:ENSMUSG00000048218; -.
DR eggNOG; ENOG502R009; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q80ZD9; -.
DR OMA; LNQSNAH; -.
DR OrthoDB; 496131at2759; -.
DR PhylomeDB; Q80ZD9; -.
DR TreeFam; TF326838; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 105827; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Amigo2; mouse.
DR PRO; PR:Q80ZD9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80ZD9; protein.
DR Bgee; ENSMUSG00000048218; Expressed in metanephric ureteric bud and 145 other tissues.
DR ExpressionAtlas; Q80ZD9; baseline and differential.
DR Genevisible; Q80ZD9; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031283; AMIGO.
DR InterPro; IPR031286; AMIGO2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24368; PTHR24368; 1.
DR PANTHER; PTHR24368:SF209; PTHR24368:SF209; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Nucleus;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..519
FT /note="Amphoterin-induced protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014510"
FT TOPO_DOM 39..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..67
FT /note="LRRNT"
FT REPEAT 68..89
FT /note="LRR 1"
FT REPEAT 93..114
FT /note="LRR 2"
FT REPEAT 117..138
FT /note="LRR 3"
FT REPEAT 141..162
FT /note="LRR 4"
FT REPEAT 165..186
FT /note="LRR 5"
FT REPEAT 192..213
FT /note="LRR 6"
FT DOMAIN 227..283
FT /note="LRRCT"
FT DOMAIN 288..378
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 498..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 44..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 231..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 233..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 309..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 519 AA; 57562 MW; 0E9DD3FFA20C0A06 CRC64;
MSLRFHTLPT LPRAVKPGCR ELLCLLVIAV MVSPSASGMC PTACICATDI VSCTNKNLSK
VPGNLFRLIK RLDLSYNRIG LLDADWIPVS FVKLSTLILR HNNITSISTG SFSTTPNLKC
LDLSSNRLKS VKSATFQELK ALEVLLLYNN HISYLDPAAF GGLSHLQKLY LSGNFLTQFP
MDLYTGRFKL ADLTFLDVSY NRIPSIPMHH INLVPGRQLR GIYLHGNPFV CDCSLYSLLI
FWYRRHFSSV MDFKNDYTCR LWSDSRHSHQ LQLLQESFLN CSYSVINGSF HALGFIHEAQ
VGERAIVHCD SKTGNGNTDF IWVGPDNRLL EPDKDMGNFR VFYNGSLVIE NPGFEDAGVY
SCIAMNRQRL LNETVDIMIN VSNFTINRSH AHEAFNTAFT TLAACVASIV LVLLYLYLTP
CPCKCKAKRQ KNTLSQSSAH SSILSPGPTG DASADDRKAG KRVVFLEPLK DTAAGQNGKV
KLFPSETVIA EGILKSTRAK SDSDSVNSVF SDTPFVAST
