AMGO2_RAT
ID AMGO2_RAT Reviewed; 520 AA.
AC Q7TNJ4; Q80ZD6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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:AAO48951.1};
GN Synonyms=Ali1 {ECO:0000312|EMBL:BAC81186.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO48951.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND
RP INTERACTION WITH AMIGO1 AND AMIGO3.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAO48951.1};
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:0000305, ECO:0000312|EMBL:BAC81186.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar {ECO:0000269|PubMed:12843293};
RC TISSUE=Cerebellum {ECO:0000269|PubMed:12843293};
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.
CC {ECO:0000269|PubMed:12629050, ECO:0000269|PubMed:12843293}.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3.
CC {ECO:0000269|PubMed:12629050}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:12843293}.
CC Note=Associated with nucleus as well as plasma membrane. Restricted to
CC somata of cerebellar as well as hippocampal neurons.
CC -!- TISSUE SPECIFICITY: Highest levels in the lung. High levels in
CC cerebellar granule neurons and Purkinje cells. Also in pyramidal cells
CC between CA1 and CA3 regions of the hippocampus and granule cells of the
CC dentate gyrus. {ECO:0000269|PubMed:12629050,
CC ECO:0000269|PubMed:12843293}.
CC -!- DEVELOPMENTAL STAGE: High level expression in cerebellum of newborn
CC rats is down-regulated to 50% by postnatal day 14.
CC {ECO:0000269|PubMed:12843293}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237730; AAO48951.1; -; mRNA.
DR EMBL; AB078879; BAC81186.1; -; mRNA.
DR RefSeq; NP_877968.2; NM_182816.2.
DR RefSeq; XP_006242352.1; XM_006242290.2.
DR RefSeq; XP_017450269.1; XM_017594780.1.
DR RefSeq; XP_017450270.1; XM_017594781.1.
DR AlphaFoldDB; Q7TNJ4; -.
DR SMR; Q7TNJ4; -.
DR STRING; 10116.ENSRNOP00000009199; -.
DR GlyGen; Q7TNJ4; 9 sites.
DR PaxDb; Q7TNJ4; -.
DR PRIDE; Q7TNJ4; -.
DR GeneID; 300186; -.
DR KEGG; rno:300186; -.
DR UCSC; RGD:727911; rat.
DR CTD; 347902; -.
DR RGD; 727911; Amigo2.
DR eggNOG; ENOG502R009; Eukaryota.
DR InParanoid; Q7TNJ4; -.
DR OrthoDB; 496131at2759; -.
DR PhylomeDB; Q7TNJ4; -.
DR TreeFam; TF326838; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q7TNJ4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IPI:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IPI:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031283; AMIGO.
DR InterPro; IPR031286; AMIGO2.
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 SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 5.
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..37
FT /evidence="ECO:0000255"
FT CHAIN 38..520
FT /note="Amphoterin-induced protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014512"
FT TOPO_DOM 38..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..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 437..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
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"
FT CONFLICT 487
FT /note="K -> E (in Ref. 2; AAO48951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 57759 MW; 9C0B8009DB35089B CRC64;
MSLRFHTLPT LPRAVKPGCR ELLCLLVIAV MVSPSSSGLC PTACICATDI VSCTNKNLSK
VPGNLFRLIK RLDLSYNRIG LLDADWIPVS FVKLSTLIVR HNNITSISTG SFSTTPNLKC
LDLSSNRLKS VKSAMFQELK VLEVLLLYNN HISYLDPAAF GGLSHLQKLY LSGNFLTKFP
MDLYVGRFKL ADLTFLDVSY NQIASIPMHH INLVPGKQLR GIFLHGNPFV CDCSLYSLLT
FWYRRHFNSV TDFKHDYTCR LWLDSRHSHQ LLLLQDSFLN CSHSVINGSF HALGFIHEAQ
VGERAIVHCD GKTGNGNTDF IWVGPDNRLL EPDKDTGNFR VFYNGSLVIE NPGFEDAGVY
SCIAMNRQRL LNETVDIMIN VSNFTINRSH HAHEAFNTAF TTLAACVVSI VLVLLYLYLT
PCPCKCRDKR QKNALNQSNA HSSILSPGPT RDASAEDRKA GKRVVFLEPL KDPAVGQNGK
VKLVPSKTVI AEGILKSSRA KSDSDSVNSV FSDTPFVAST
