AMGO3_RAT
ID AMGO3_RAT Reviewed; 508 AA.
AC Q80ZD5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Amphoterin-induced protein 3;
DE AltName: Full=AMIGO-3;
DE AltName: Full=Alivin-3;
DE Flags: Precursor;
GN Name=Amigo3 {ECO:0000312|EMBL:AAO48952.1, ECO:0000312|RGD:631413};
GN Synonyms=Ali3 {ECO:0000250|UniProtKB:Q8C2S7};
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:AAO48952.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH AMIGO1 AND AMIGO2.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAO48952.1};
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).
CC -!- FUNCTION: May mediate heterophilic cell-cell interaction. May
CC contribute to signal transduction through its intracellular domain.
CC {ECO:0000303|PubMed:12629050}.
CC -!- SUBUNIT: Binds AMIGO1 or AMIGO2.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237731; AAO48952.1; -; mRNA.
DR RefSeq; NP_835280.1; NM_178144.1.
DR AlphaFoldDB; Q80ZD5; -.
DR SMR; Q80ZD5; -.
DR GlyGen; Q80ZD5; 5 sites.
DR PRIDE; Q80ZD5; -.
DR Ensembl; ENSRNOT00000100102; ENSRNOP00000093720; ENSRNOG00000064183.
DR Ensembl; ENSRNOT00000101890; ENSRNOP00000082203; ENSRNOG00000064183.
DR Ensembl; ENSRNOT00000114148; ENSRNOP00000076680; ENSRNOG00000064183.
DR Ensembl; ENSRNOT00000118165; ENSRNOP00000081738; ENSRNOG00000064183.
DR GeneID; 316003; -.
DR KEGG; rno:316003; -.
DR UCSC; RGD:631413; rat.
DR CTD; 386724; -.
DR RGD; 631413; Amigo3.
DR GeneTree; ENSGT00950000183146; -.
DR InParanoid; Q80ZD5; -.
DR OrthoDB; 564038at2759; -.
DR PhylomeDB; Q80ZD5; -.
DR PRO; PR:Q80ZD5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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; IPI:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
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; IPR031285; AMIGO3.
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; 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:SF62; PTHR24368:SF62; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..508
FT /note="Amphoterin-induced protein 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014515"
FT TOPO_DOM 20..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 86..107
FT /note="LRR 2"
FT REPEAT 110..131
FT /note="LRR 3"
FT REPEAT 134..155
FT /note="LRR 4"
FT REPEAT 158..178
FT /note="LRR 5"
FT REPEAT 184..207
FT /note="LRR 6"
FT DOMAIN 219..275
FT /note="LRRCT"
FT DOMAIN 279..370
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 38..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 223..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 225..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 300..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 508 AA; 55565 MW; FD983CE97D83392D CRC64;
MAWLVLLGLL LCMLGAGSGT SDLEGVLPPD PHNCPNKCVC AADVLSCAGR GLQDLPAALP
ATAAELDLSH NALKRLHPGW LAPLSRLRAL YLGYNKLDVL GRGVFTNASG LRILDLSSNL
LRRLRTYDLD GLEELEKLLL FNNRLMHLDL DAFQGLSMLS HLYLSCNELS SFSFNHLHGL
GLTRLRTLDL SSNWLGHVSV PELAALPTFL KNRLYLHNNP LPCDCSLYHL LRRWHQRGLS
ALHDFEREYT CLAFKVAESR VRFFEHSRVF KNCSVAAAPG LELPEEELHT HVGQSLRLFC
NTTVPAARVA WVSPKNELLV APGSQDGSIA VLADGSLAIG RVQEQHAGLF VCLASGPRLH
HNQTLEYNVS VHKPRPEPEA FNTGFTTLLG CIVGLVLVLL YLFAPPCRGC CRCCRRACRN
RCWPRASSPL QELSAQSSVL STTPPDAPSR KASVHKHVAF LEPGKKGLNG RVQLAVAEDF
DLCNPMGLQL KAGSESASST GSEGLMMS
