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P58355 (S45A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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:
Membrane-associated transporter protein
Alternative name(s):
Melanoma antigen AIM1
Short name=Protein AIM-1
Protein underwhite
Solute carrier family 45 member 2
Gene names
Name:Slc45a2
Synonyms:Aim1, Matp, uw
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Melanocyte differentiation antigen. May transport substances required for melanin biosynthesis By similarity.

Subcellular location

Melanosome membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Melanocytes, eyes, kidney and uterus.

Involvement in disease

Defects in Slc45a2 are the cause of the UW-dbr phenotype that results in loss of nearly all pigmentation in the homozygous state.

Sequence similarities

Belongs to the glycoside-pentoside-hexuronide (GPH) cation symporter transporter (TC 2.A.2) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Membrane-associated transporter protein
PRO_0000122518

Regions

Topological domain1 – 4545Cytoplasmic Potential
Transmembrane46 – 6621Helical; Name=1; Potential
Topological domain67 – 682Extracellular Potential
Transmembrane69 – 8921Helical; Name=2; Potential
Topological domain90 – 10516Cytoplasmic Potential
Transmembrane106 – 12621Helical; Name=3; Potential
Topological domain127 – 13812Extracellular Potential
Transmembrane139 – 15921Helical; Name=4; Potential
Topological domain160 – 18425Cytoplasmic Potential
Transmembrane185 – 20521Helical; Name=5; Potential
Topological domain206 – 21611Extracellular Potential
Transmembrane217 – 23721Helical; Name=6; Potential
Topological domain238 – 31881Cytoplasmic Potential
Transmembrane319 – 33921Helical; Name=7; Potential
Topological domain340 – 36627Extracellular Potential
Transmembrane367 – 38721Helical; Name=8; Potential
Topological domain388 – 39811Cytoplasmic Potential
Transmembrane399 – 41921Helical; Name=9; Potential
Topological domain420 – 4256Extracellular Potential
Transmembrane426 – 44621Helical; Name=10; Potential
Topological domain447 – 47731Cytoplasmic Potential
Transmembrane478 – 49821Helical; Name=11; Potential
Topological domain499 – 5046Extracellular Potential
Transmembrane505 – 52521Helical; Name=12; Potential
Topological domain526 – 5305Cytoplasmic Potential

Amino acid modifications

Glycosylation3561N-linked (GlcNAc...) Potential

Natural variations

Natural variant1531D → N in UW-dbr. Ref.2
Natural variant4351S → P in UW-dbr. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P58355 [UniParc].

Last modified November 16, 2001. Version 1.
Checksum: F4EDEAD07916D9FC

FASTA53057,961
        10         20         30         40         50         60 
MSGSNGPTDT HTYQSLAEDC PFGSVEQPKR STGRLVMHSM AMFGREFCYA VEAAYVTPVL 

        70         80         90        100        110        120 
LSVGLPKSLY SMVWLLSPIL GFLLQPVVGS ASDHCRARWG RRRPYILTLA IMMLLGMALY 

       130        140        150        160        170        180 
LNGDAVVSAL VANPRQKLIW AISITMVGVV LFDFSADFID GPIKAYLFDV CSHQDKEKGL 

       190        200        210        220        230        240 
HYHALFTGFG GALGYILGAI DWVHLDLGRL LGTEFQVMFF FSALVLILCF ITHLCSIPEA 

       250        260        270        280        290        300 
PLRDAATDPP SQQDPQGSSL SASGMHEYGS IEKVKNGGAD TEQPVQEWKN KKPSGQSQRT 

       310        320        330        340        350        360 
MSMKSLLRAL VNMPSHYRCL CVSHLIGWTA FLSNMLFFTD FMGQIVYHGD PYGAHNSTEF 

       370        380        390        400        410        420 
LIYERGVEVG CWGLCINSVF SSVYSYFQKA MVSYIGLKGL YFMGYLLFGL GTGFIGLFPN 

       430        440        450        460        470        480 
VYSTLVLCSM FGVMSSTLYT VPFNLIAEYH REEEKEKGQE APGGPDNQGR GKGVDCAALT 

       490        500        510        520        530 
CMVQLAQILV GGGLGFLVNM AGSVVVVVIT ASAVSLIGCC FVALFVRYVD 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in the gene encoding B, a novel transporter protein, reduce melanin content in medaka."
Fukamachi S., Shimada A., Shima A.
Nat. Genet. 28:381-385(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ddY.
Tissue: Eye, Kidney and Uterus.
[2]"Mutations in the human orthologue of the mouse underwhite gene (uw) underlie a new form of oculocutaneous albinism, OCA4."
Newton J.M., Cohen-Barak O., Hagiwara N., Gardner J.M., Davisson M.T., King R.A., Brilliant M.H.
Am. J. Hum. Genet. 69:981-988(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS UW-DBR ASN-153 AND PRO-435.
[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.
Tissue: Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF360357 mRNA. Translation: AAK81713.1.
AK029155 mRNA. Translation: BAC26330.1.
RefSeqNP_444307.1. NM_053077.3.
XP_006520111.1. XM_006520048.1.
UniGeneMm.138278.

3D structure databases

ProteinModelPortalP58355.
SMRP58355. Positions 10-38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000022851.

PTM databases

PhosphoSiteP58355.

Proteomic databases

PRIDEP58355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022851; ENSMUSP00000022851; ENSMUSG00000022243.
GeneID22293.
KEGGmmu:22293.
UCSCuc007vgx.1. mouse.

Organism-specific databases

CTD51151.
MGIMGI:2153040. Slc45a2.

Phylogenomic databases

eggNOGNOG317436.
HOGENOMHOG000128553.
HOVERGENHBG018570.
InParanoidP58355.
KOK15378.
OMAMGGNSGQ.
PhylomeDBP58355.
TreeFamTF325412.

Gene expression databases

BgeeP58355.
CleanExMM_SLC45A2.
GenevestigatorP58355.

Family and domain databases

InterProIPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
ProtoNetSearch...

Other

ChiTaRSSLC45A2. mouse.
NextBio302439.
PROP58355.
SOURCESearch...

Entry information

Entry nameS45A2_MOUSE
AccessionPrimary (citable) accession number: P58355
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 92 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