AMGO1_RAT
ID AMGO1_RAT Reviewed; 493 AA.
AC Q80ZD7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Amphoterin-induced protein 1;
DE AltName: Full=AMIGO-1;
DE AltName: Full=Alivin-2;
DE Flags: Precursor;
GN Name=Amigo1 {ECO:0000250|UniProtKB:Q80ZD8};
GN Synonyms=Ali2 {ECO:0000250|UniProtKB:Q80ZD8},
GN Amigo {ECO:0000303|PubMed:12629050};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, SUBUNIT, AND INTERACTION WITH AMIGO2 AND AMIGO3.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAO48950.1};
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes growth and fasciculation of neurites from cultured
CC hippocampal neurons. May be involved in fasciculation as well as
CC myelination of developing neural axons. May have a role in regeneration
CC as well as neural plasticity in the adult nervous system. May mediate
CC homophilic as well as heterophilic cell-cell interaction and contribute
CC to signal transduction through its intracellular domain
CC (PubMed:12629050). Assembled with KCNB1 modulates the gating
CC characteristics of the delayed rectifier voltage-dependent potassium
CC channel KCNB1 (By similarity). {ECO:0000250|UniProtKB:Q80ZD8,
CC ECO:0000269|PubMed:12629050, ECO:0000303|PubMed:12629050}.
CC -!- SUBUNIT: Homodimer, and heterodimer with AMIGO2 and AMIGO3
CC (PubMed:12629050). Interacts with KCNB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q80ZD8, ECO:0000269|PubMed:12629050}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80ZD8};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q80ZD8}.
CC Perikaryon {ECO:0000250|UniProtKB:Q80ZD8}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q80ZD8}. Cell projection, axon
CC {ECO:0000269|PubMed:12629050}. Note=Associated with axons of neuronal
CC cells (PubMed:12629050). Colocalizes with KCNB1 at high-density
CC somatodendritic clusters on the surface of hippocampal and cortical
CC neurons (By similarity). {ECO:0000250|UniProtKB:Q80ZD8}.
CC -!- DEVELOPMENTAL STAGE: Expressed at moderate levels in the central
CC nervous system of stage 13-14 embryos. Highest levels at this stage in
CC fiber tracts from dorsal root ganglia and trigeminal ganglion to the
CC spinal cord as well as in fibers on both sides of the Purkinje cell
CC layer of the cerebellum. Expression is down-regulated during postnatal
CC stages P6 to P10 followed by up-regulation at the onset of myelination.
CC High level expression in most myelinated axon tracts of the adult
CC including cerebellum, pons, medulla, and spinal cord as well as in
CC nonmyelinated fiber tracts in the striatum lucidum CA3 region of the
CC hippocampus. {ECO:0000269|PubMed:12629050}.
CC -!- INDUCTION: By HMGB1/amphoterin; in cultured hippocampal neurons.
CC {ECO:0000269|PubMed:12629050}.
CC -!- DOMAIN: The LRR repeat region mediates homodimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO family.
CC {ECO:0000305}.
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DR EMBL; AY237729; AAO48950.1; -; mRNA.
DR RefSeq; NP_996764.1; NM_206881.1.
DR RefSeq; XP_006233202.1; XM_006233140.2.
DR RefSeq; XP_008759613.1; XM_008761391.1.
DR AlphaFoldDB; Q80ZD7; -.
DR SMR; Q80ZD7; -.
DR IntAct; Q80ZD7; 1.
DR MINT; Q80ZD7; -.
DR STRING; 10116.ENSRNOP00000066608; -.
DR GlyGen; Q80ZD7; 5 sites.
DR iPTMnet; Q80ZD7; -.
DR PhosphoSitePlus; Q80ZD7; -.
DR PaxDb; Q80ZD7; -.
DR PRIDE; Q80ZD7; -.
DR ABCD; Q80ZD7; 4 sequenced antibodies.
DR Ensembl; ENSRNOT00000074725; ENSRNOP00000066608; ENSRNOG00000045665.
DR GeneID; 295365; -.
DR KEGG; rno:295365; -.
DR UCSC; RGD:1303079; rat.
DR CTD; 57463; -.
DR RGD; 1303079; Amigo1.
DR eggNOG; ENOG502QVUQ; Eukaryota.
DR GeneTree; ENSGT00950000183146; -.
DR HOGENOM; CLU_030478_0_0_1; -.
DR InParanoid; Q80ZD7; -.
DR OMA; VFSDTPM; -.
DR OrthoDB; 671228at2759; -.
DR PhylomeDB; Q80ZD7; -.
DR PRO; PR:Q80ZD7; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000045665; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q80ZD7; RN.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:1990030; C:pericellular basket; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; IDA:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:1905232; P:cellular response to L-glutamate; IDA: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:0042552; P:myelination; IEP:UniProtKB.
DR GO; GO:0106030; P:neuron projection fasciculation; IDA:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IMP:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR031283; AMIGO.
DR InterPro; IPR031284; AMIGO1.
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; IPR013098; Ig_I-set.
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:SF1; PTHR24368:SF1; 1.
DR Pfam; PF07679; I-set; 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; Cell projection; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..493
FT /note="Amphoterin-induced protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014508"
FT TOPO_DOM 28..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 87..108
FT /note="LRR 2"
FT REPEAT 111..132
FT /note="LRR 3"
FT REPEAT 135..156
FT /note="LRR 4"
FT REPEAT 159..179
FT /note="LRR 5"
FT REPEAT 186..206
FT /note="LRR 6"
FT DOMAIN 221..272
FT /note="LRRCT"
FT DOMAIN 269..353
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 405..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80ZD8"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
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 225..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 290..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 493 AA; 55283 MW; F7FAAE936B2337D4 CRC64;
MQPQRDLRGL WLLLLSLFLL LFEVARAGRP VVSCPANCLC ASNILSCSKQ QLPNVPQSLP
GYTALLDLSH NNLSRLKAEW TPTRLTNLHS LLLSHNHLNF ISSEAFVPVP NLRYLDLSSN
HLHTLDEFLF SGLQALEVLL LYNNHIVVVD RNAFEDMAQL QKLYLSQNMI SRFPLELIKD
ANRLPKLTLL DLSSNKLKKL PLTDLQKLPA WVKNGLYLHN NPLECDCKLY QLFSHWQYRQ
LSSVMDFQED LYCVHSKKLH NVFSLDFFNC SEYKESAWEA HLGDTLTITC DTKQQGMTKV
WVTPSNEQVL NQGANGTVTV SEDGNLHFKE VQVEDGGVYT CYAMGETFNE TLSVELKVYN
FTLHGHHDTL NTAYTTLVGC ILSVVLVLIY LYLTPCRCWC RGVEKPSSHQ GDSLSSSMLS
TTPNHDPMAG GDKDDGFDRR VAFLEPAGPG QGQNGKLKPG NTLPVPEATG KGQRRMSDPE
SVSSVFSDTP IVV
