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Protein

Amphoterin-induced protein 1

Gene

AMIGO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.By similarity

GO - Molecular functioni

GO - Biological processi

  • axonal fasciculation Source: UniProtKB
  • axonogenesis Source: Ensembl
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  • myelination Source: UniProtKB
  • positive regulation of axonogenesis Source: UniProtKB
  • positive regulation of potassium ion transmembrane transport Source: UniProtKB
  • positive regulation of synapse assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Amphoterin-induced protein 1
Alternative name(s):
AMIGO-1
Alivin-2
Gene namesi
Name:AMIGO1Imported
Synonyms:ALI2By similarity, AMIGO1 Publication, KIAA1163Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20824. AMIGO1.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Perikaryon By similarity
  • Cell projectiondendrite By similarity
  • Cell projectionaxon By similarity

  • Note: Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal and cortical neurons. Associated with axons of neuronal cells.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 372345ExtracellularSequence analysisAdd
BLAST
Transmembranei373 – 39321HelicalSequence analysisAdd
BLAST
Topological domaini394 – 493100CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672625.

Polymorphism and mutation databases

BioMutaiAMIGO1.
DMDMi68052342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 493466Amphoterin-induced protein 1Sequence analysisPRO_0000014506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 40PROSITE-ProRule annotation
Disulfide bondi38 ↔ 47PROSITE-ProRule annotation
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Disulfide bondi225 ↔ 253PROSITE-ProRule annotation
Disulfide bondi227 ↔ 270PROSITE-ProRule annotation
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi290 ↔ 341PROSITE-ProRule annotation
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence analysis
Modified residuei477 – 4771PhosphoserineCombined sources
Modified residuei481 – 4811PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ86WK6.
MaxQBiQ86WK6.
PaxDbiQ86WK6.
PRIDEiQ86WK6.

PTM databases

iPTMnetiQ86WK6.
PhosphoSiteiQ86WK6.

Expressioni

Gene expression databases

BgeeiQ86WK6.
CleanExiHS_AMIGO1.
GenevisibleiQ86WK6. HS.

Organism-specific databases

HPAiHPA046152.

Interactioni

Subunit structurei

Homodimer, and heterodimer with AMIGO2 and AMIGO3. Interacts with KCNB1.By similarity

Protein-protein interaction databases

BioGridi121533. 26 interactions.
STRINGi9606.ENSP00000358878.

Structurei

3D structure databases

ProteinModelPortaliQ86WK6.
SMRiQ86WK6. Positions 31-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6134LRRNTAdd
BLAST
Repeati62 – 8322LRR 1Add
BLAST
Repeati87 – 10822LRR 2Add
BLAST
Repeati111 – 13222LRR 3Add
BLAST
Repeati135 – 15622LRR 4Add
BLAST
Repeati159 – 17921LRR 5Add
BLAST
Repeati186 – 20621LRR 6Add
BLAST
Domaini221 – 27252LRRCTAdd
BLAST
Domaini269 – 35385Ig-like C2-typeSequence analysisAdd
BLAST

Domaini

The LRR repeat region mediates homodimerization.By similarity

Sequence similaritiesi

Contains 6 LRR (leucine-rich) repeats.Sequence analysis
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGN4. Eukaryota.
ENOG410ZZH4. LUCA.
GeneTreeiENSGT00530000063545.
HOGENOMiHOG000231327.
HOVERGENiHBG080231.
InParanoidiQ86WK6.
OMAiCSEYKER.
OrthoDBiEOG7R8318.
PhylomeDBiQ86WK6.
TreeFamiTF326838.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR031283. AMIGO.
IPR031284. AMIGO1.
IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PANTHERiPTHR24368. PTHR24368. 1 hit.
PTHR24368:SF1. PTHR24368:SF1. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q86WK6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPHRDPRGL WLLLPSLSLL LFEVARAGRA VVSCPAACLC ASNILSCSKQ
60 70 80 90 100
QLPNVPHSLP SYTALLDLSH NNLSRLRAEW TPTRLTQLHS LLLSHNHLNF
110 120 130 140 150
ISSEAFSPVP NLRYLDLSSN QLRTLDEFLF SDLQVLEVLL LYNNHIMAVD
160 170 180 190 200
RCAFDDMAQL QKLYLSQNQI SRFPLELVKE GAKLPKLTLL DLSSNKLKNL
210 220 230 240 250
PLPDLQKLPA WIKNGLYLHN NPLNCDCELY QLFSHWQYRQ LSSVMDFQED
260 270 280 290 300
LYCMNSKKLH NVFNLSFLNC GEYKERAWEA HLGDTLIIKC DTKQQGMTKV
310 320 330 340 350
WVTPSNERVL DEVTNGTVSV SKDGSLLFQQ VQVEDGGVYT CYAMGETFNE
360 370 380 390 400
TLSVELKVHN FTLHGHHDTL NTAYTTLVGC ILSVVLVLIY LYLTPCRCWC
410 420 430 440 450
RGVEKPSSHQ GDSLSSSMLS TTPNHDPMAG GDKDDGFDRR VAFLEPAGPG
460 470 480 490
QGQNGKLKPG NTLPVPEATG KGQRRMSDPE SVSSVFSDTP IVV
Length:493
Mass (Da):55,239
Last modified:June 1, 2003 - v1
Checksum:i8685B358570D9455
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti454 – 4541N → S in AAH40879 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237007 mRNA. Translation: AAO48948.1.
AK295678 mRNA. Translation: BAG58535.1.
AL355145 Genomic DNA. Translation: CAI22942.1.
BC040879 mRNA. Translation: AAH40879.1.
AB032989 mRNA. Translation: BAA86477.1.
CCDSiCCDS30795.1.
RefSeqiNP_065754.2. NM_020703.2.
XP_011540114.1. XM_011541812.1.
UniGeneiHs.726479.

Genome annotation databases

EnsembliENST00000369862; ENSP00000358878; ENSG00000181754.
ENST00000369864; ENSP00000358880; ENSG00000181754.
GeneIDi57463.
KEGGihsa:57463.
UCSCiuc001dxx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY237007 mRNA. Translation: AAO48948.1.
AK295678 mRNA. Translation: BAG58535.1.
AL355145 Genomic DNA. Translation: CAI22942.1.
BC040879 mRNA. Translation: AAH40879.1.
AB032989 mRNA. Translation: BAA86477.1.
CCDSiCCDS30795.1.
RefSeqiNP_065754.2. NM_020703.2.
XP_011540114.1. XM_011541812.1.
UniGeneiHs.726479.

3D structure databases

ProteinModelPortaliQ86WK6.
SMRiQ86WK6. Positions 31-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121533. 26 interactions.
STRINGi9606.ENSP00000358878.

PTM databases

iPTMnetiQ86WK6.
PhosphoSiteiQ86WK6.

Polymorphism and mutation databases

BioMutaiAMIGO1.
DMDMi68052342.

Proteomic databases

EPDiQ86WK6.
MaxQBiQ86WK6.
PaxDbiQ86WK6.
PRIDEiQ86WK6.

Protocols and materials databases

DNASUi57463.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369862; ENSP00000358878; ENSG00000181754.
ENST00000369864; ENSP00000358880; ENSG00000181754.
GeneIDi57463.
KEGGihsa:57463.
UCSCiuc001dxx.5. human.

Organism-specific databases

CTDi57463.
GeneCardsiAMIGO1.
HGNCiHGNC:20824. AMIGO1.
HPAiHPA046152.
MIMi615689. gene.
neXtProtiNX_Q86WK6.
PharmGKBiPA142672625.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGN4. Eukaryota.
ENOG410ZZH4. LUCA.
GeneTreeiENSGT00530000063545.
HOGENOMiHOG000231327.
HOVERGENiHBG080231.
InParanoidiQ86WK6.
OMAiCSEYKER.
OrthoDBiEOG7R8318.
PhylomeDBiQ86WK6.
TreeFamiTF326838.

Miscellaneous databases

ChiTaRSiAMIGO1. human.
GenomeRNAii57463.
PROiQ86WK6.
SOURCEiSearch...

Gene expression databases

BgeeiQ86WK6.
CleanExiHS_AMIGO1.
GenevisibleiQ86WK6. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR031283. AMIGO.
IPR031284. AMIGO1.
IPR000483. Cys-rich_flank_reg_C.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PANTHERiPTHR24368. PTHR24368. 1 hit.
PTHR24368:SF1. PTHR24368:SF1. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AMIGO, a transmembrane protein implicated in axon tract development, defines a novel protein family with leucine-rich repeats."
    Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A., Rauvala H.
    J. Cell Biol. 160:963-973(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocytic leukemia1 Publication.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: OvaryImported.
  5. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-493.
    Tissue: BrainImported.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiAMGO1_HUMAN
AccessioniPrimary (citable) accession number: Q86WK6
Secondary accession number(s): B4DIM3, Q8IW71, Q9ULQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.