AMGO2_HUMAN
ID AMGO2_HUMAN Reviewed; 522 AA.
AC Q86SJ2; Q4VBP6; Q7Z4A0; Q96CN8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Amphoterin-induced protein 2;
DE AltName: Full=AMIGO-2;
DE AltName: Full=Alivin-1;
DE AltName: Full=Differentially expressed in gastric adenocarcinomas;
DE Short=DEGA;
DE Flags: Precursor;
GN Name=AMIGO2 {ECO:0000312|EMBL:AAH47595.1};
GN Synonyms=ALI1 {ECO:0000312|EMBL:BAC81189.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:AAO48946.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrosarcoma {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:BAC81189.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAC81189.1};
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).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAR83271.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15107827; DOI=10.1038/sj.onc.1207681;
RA Rabenau K.E., O'Toole J.M., Bassi R., Kotanides H., Witte L., Ludwig D.L.,
RA Pereira D.S.;
RT "DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
RT expressed in human gastric adenocarcinoma: effects on ploidy, chromosomal
RT stability, cell adhesion/migration and tumorigenicity.";
RL Oncogene 23:5056-5067(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5] {ECO:0000312|EMBL:AAH47595.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH47595.1}, and
RC Uterus {ECO:0000312|EMBL:AAH14103.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
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. May
CC be required for tumorigenesis of a subset of gastric adenocarcinomas.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3. {ECO:0000250}.
CC -!- INTERACTION:
CC Q86SJ2; O00555: CACNA1A; NbExp=2; IntAct=EBI-3866830, EBI-766279;
CC Q86SJ2; Q6PL24: TMED8; NbExp=3; IntAct=EBI-3866830, EBI-11603430;
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 levels in breast, ovary, cervix, and
CC uterus. Lower levels in lung, colon, and rectum. Differentially
CC expressed in 56% of thyroid, 57% of pancreatic and 45% of stomach
CC cancers. {ECO:0000269|PubMed:15107827}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237005; AAO48946.1; -; mRNA.
DR EMBL; AB079074; BAC81188.1; -; mRNA.
DR EMBL; AB080610; BAC81189.1; -; mRNA.
DR EMBL; AY454159; AAR83271.1; -; mRNA.
DR EMBL; AL833007; CAH56293.1; -; mRNA.
DR EMBL; BC014103; AAH14103.2; -; mRNA.
DR EMBL; BC047595; AAH47595.1; -; mRNA.
DR EMBL; BC095477; AAH95477.1; -; mRNA.
DR CCDS; CCDS8751.1; -.
DR RefSeq; NP_001137140.1; NM_001143668.1.
DR RefSeq; NP_862830.1; NM_181847.4.
DR RefSeq; XP_005268894.1; XM_005268837.3.
DR AlphaFoldDB; Q86SJ2; -.
DR SMR; Q86SJ2; -.
DR BioGRID; 131497; 32.
DR IntAct; Q86SJ2; 6.
DR STRING; 9606.ENSP00000266581; -.
DR GlyConnect; 1007; 4 N-Linked glycans (1 site).
DR GlyGen; Q86SJ2; 9 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q86SJ2; -.
DR PhosphoSitePlus; Q86SJ2; -.
DR SwissPalm; Q86SJ2; -.
DR BioMuta; AMIGO2; -.
DR DMDM; 68052338; -.
DR EPD; Q86SJ2; -.
DR jPOST; Q86SJ2; -.
DR MassIVE; Q86SJ2; -.
DR MaxQB; Q86SJ2; -.
DR PaxDb; Q86SJ2; -.
DR PeptideAtlas; Q86SJ2; -.
DR PRIDE; Q86SJ2; -.
DR ProteomicsDB; 69596; -.
DR Antibodypedia; 13397; 242 antibodies from 31 providers.
DR DNASU; 347902; -.
DR Ensembl; ENST00000266581.4; ENSP00000266581.4; ENSG00000139211.7.
DR Ensembl; ENST00000429635.1; ENSP00000406020.1; ENSG00000139211.7.
DR Ensembl; ENST00000550413.2; ENSP00000449034.1; ENSG00000139211.7.
DR GeneID; 347902; -.
DR KEGG; hsa:347902; -.
DR MANE-Select; ENST00000550413.2; ENSP00000449034.1; NM_001370299.1; NP_001357228.1.
DR UCSC; uc001rpk.4; human.
DR CTD; 347902; -.
DR DisGeNET; 347902; -.
DR GeneCards; AMIGO2; -.
DR HGNC; HGNC:24073; AMIGO2.
DR HPA; ENSG00000139211; Low tissue specificity.
DR MIM; 615690; gene.
DR neXtProt; NX_Q86SJ2; -.
DR OpenTargets; ENSG00000139211; -.
DR PharmGKB; PA142672626; -.
DR VEuPathDB; HostDB:ENSG00000139211; -.
DR eggNOG; ENOG502R009; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q86SJ2; -.
DR OMA; LNQSNAH; -.
DR OrthoDB; 496131at2759; -.
DR PhylomeDB; Q86SJ2; -.
DR TreeFam; TF326838; -.
DR PathwayCommons; Q86SJ2; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q86SJ2; -.
DR BioGRID-ORCS; 347902; 12 hits in 1086 CRISPR screens.
DR GenomeRNAi; 347902; -.
DR Pharos; Q86SJ2; Tbio.
DR PRO; PR:Q86SJ2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86SJ2; protein.
DR Bgee; ENSG00000139211; Expressed in blood vessel layer and 188 other tissues.
DR ExpressionAtlas; Q86SJ2; baseline and differential.
DR Genevisible; Q86SJ2; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
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:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
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; 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; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
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..39
FT /evidence="ECO:0000255"
FT CHAIN 40..522
FT /note="Amphoterin-induced protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014509"
FT TOPO_DOM 40..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..68
FT /note="LRRNT"
FT REPEAT 69..90
FT /note="LRR 1"
FT REPEAT 94..115
FT /note="LRR 2"
FT REPEAT 118..139
FT /note="LRR 3"
FT REPEAT 142..163
FT /note="LRR 4"
FT REPEAT 166..187
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT DOMAIN 228..284
FT /note="LRRCT"
FT DOMAIN 289..379
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 501..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 45..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 232..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 310..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 522 AA; 57934 MW; 20A86E3D82C05B9B CRC64;
MSLRVHTLPT LLGAVVRPGC RELLCLLMIT VTVGPGASGV CPTACICATD IVSCTNKNLS
KVPGNLFRLI KRLDLSYNRI GLLDSEWIPV SFAKLNTLIL RHNNITSIST GSFSTTPNLK
CLDLSSNKLK TVKNAVFQEL KVLEVLLLYN NHISYLDPSA FGGLSQLQKL YLSGNFLTQF
PMDLYVGRFK LAELMFLDVS YNRIPSMPMH HINLVPGKQL RGIYLHGNPF VCDCSLYSLL
VFWYRRHFSS VMDFKNDYTC RLWSDSRHSR QVLLLQDSFM NCSDSIINGS FRALGFIHEA
QVGERLMVHC DSKTGNANTD FIWVGPDNRL LEPDKEMENF YVFHNGSLVI ESPRFEDAGV
YSCIAMNKQR LLNETVDVTI NVSNFTVSRS HAHEAFNTAF TTLAACVASI VLVLLYLYLT
PCPCKCKTKR QKNMLHQSNA HSSILSPGPA SDASADERKA GAGKRVVFLE PLKDTAAGQN
GKVRLFPSEA VIAEGILKST RGKSDSDSVN SVFSDTPFVA ST
