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Q8C2S7 (AMGO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amphoterin-induced protein 3
Alternative name(s):
AMIGO-3
Alivin-3
Gene names
Name:Amigo3
Synonyms:Ali3, Kiaa1851
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain By similarity. UniProtKB Q80ZD5

Subunit structure

Binds AMIGO1 or AMIGO2 By similarity. Ref.1

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the immunoglobulin superfamily. AMIGO family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 6 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Sequence caution

The sequence BAC26035.1 differs from that shown. Reason: Frameshift at position 224.

The sequence BAC98266.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 508489Amphoterin-induced protein 3
PRO_0000014514

Regions

Topological domain20 – 383364Extracellular Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 508104Cytoplasmic Potential
Domain25 – 6137LRRNT
Repeat62 – 8322LRR 1
Repeat86 – 10722LRR 2
Repeat110 – 13324LRR 3
Repeat134 – 15522LRR 4
Repeat158 – 17821LRR 5
Repeat184 – 20724LRR 6
Domain219 – 27557LRRCT
Domain279 – 37092Ig-like C2-type

Amino acid modifications

Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 40 By similarity
Disulfide bond38 ↔ 47 By similarity
Disulfide bond223 ↔ 251 By similarity
Disulfide bond225 ↔ 273 By similarity
Disulfide bond300 ↔ 352 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C2S7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 31334E42F91810C5

FASTA50855,625
        10         20         30         40         50         60 
MAWLVLSGIL LCMLGAGLGT SDLEDVLPPA PHNCPDICIC AADVLSCAGR GLQDLPVALP 

        70         80         90        100        110        120 
TTAAELDLSH NALKRLHPGW LAPLSRLRAL HLGYNKLEVL GHGAFTNASG LRTLDLSSNM 

       130        140        150        160        170        180 
LRMLHTHDLD GLEELEKLLL FNNSLMHLDL DAFQGLRMLS HLYLSCNELS SFSFNHLHGL 

       190        200        210        220        230        240 
GLTRLRTLDL SSNWLKHISI PELAALPTYL KNRLYLHNNP LPCDCSLYHL LRRWHQRGLS 

       250        260        270        280        290        300 
ALHDFEREYT CLVFKVSESR VRFFEHSRVF KNCSVAAAPG LELPEEQLHA QVGQSLRLFC 

       310        320        330        340        350        360 
NTSVPATRVA WVSPKNELLV APASQDGSIA VLADGSLAIG RVQEQHAGVF VCLASGPRLH 

       370        380        390        400        410        420 
HNQTLEYNVS VQKARPEPET FNTGFTTLLG CIVGLVLVLL YLFAPPCRGC CHCCQRACRN 

       430        440        450        460        470        480 
RCWPRASSPL QELSAQSSML STTPPDAPSR KASVHKHVVF LEPGKKGLNG RVQLAVAEDF 

       490        500 
DLCNPMGLQL KAGSESASST GSEGLVMS 

« Hide

References

« Hide 'large scale' references
[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], SUBUNIT, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Cerebellum.
[2]Ono T.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Skin and Thymus.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic tail.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY237004 mRNA. Translation: AAO48945.1.
AB167510 mRNA. Translation: BAD12542.1.
AK028619 mRNA. Translation: BAC26035.1. Frameshift.
AK088051 mRNA. Translation: BAC40120.1.
AK129456 mRNA. Translation: BAC98266.1. Different initiation.
RefSeqNP_796249.1. NM_177275.4.
UniGeneMm.449806.

3D structure databases

ProteinModelPortalQ8C2S7.
SMRQ8C2S7. Positions 14-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000082137.

PTM databases

PhosphoSiteQ8C2S7.

Proteomic databases

PRIDEQ8C2S7.

Protocols and materials databases

DNASU320844.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085060; ENSMUSP00000082137; ENSMUSG00000032593.
GeneID320844.
KEGGmmu:320844.
UCSCuc009rom.1. mouse.

Organism-specific databases

CTD386724.
MGIMGI:2444854. Amigo3.
RougeSearch...

Phylogenomic databases

eggNOGNOG146733.
GeneTreeENSGT00530000063545.
HOGENOMHOG000231327.
HOVERGENHBG080231.
InParanoidQ8C2S7.
OMAVCLATGP.
OrthoDBEOG7C8GHP.
PhylomeDBQ8C2S7.
TreeFamTF326838.

Gene expression databases

BgeeQ8C2S7.
CleanExMM_AMIGO3.
GenevestigatorQ8C2S7.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio397545.
PROQ8C2S7.
SOURCESearch...

Entry information

Entry nameAMGO3_MOUSE
AccessionPrimary (citable) accession number: Q8C2S7
Secondary accession number(s): Q6ZPH1, Q8CEB3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot