S45A2_MOUSE
ID S45A2_MOUSE Reviewed; 530 AA.
AC P58355;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Membrane-associated transporter protein;
DE AltName: Full=Melanoma antigen AIM1;
DE Short=Protein AIM-1;
DE AltName: Full=Protein underwhite;
DE AltName: Full=Solute carrier family 45 member 2;
GN Name=Slc45a2; Synonyms=Aim1, Matp, uw;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Eye, Kidney, and Uterus;
RX PubMed=11479596; DOI=10.1038/ng584;
RA Fukamachi S., Shimada A., Shima A.;
RT "Mutations in the gene encoding B, a novel transporter protein, reduce
RT melanin content in medaka.";
RL Nat. Genet. 28:381-385(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS UW-DBR ASN-153 AND PRO-435, AND
RP INVOLVEMENT IN UW-DBR.
RX PubMed=11574907; DOI=10.1086/324340;
RA Newton J.M., Cohen-Barak O., Hagiwara N., Gardner J.M., Davisson M.T.,
RA King R.A., Brilliant M.H.;
RT "Mutations in the human orthologue of the mouse underwhite gene (uw)
RT underlie a new form of oculocutaneous albinism, OCA4.";
RL Am. J. Hum. Genet. 69:981-988(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Melanocyte differentiation antigen. May transport substances
CC required for melanin biosynthesis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Melanocytes, eyes, kidney and uterus.
CC -!- DISEASE: Note=Defects in Slc45a2 are the cause of the UW-dbr phenotype
CC that results in loss of nearly all pigmentation in the homozygous
CC state. {ECO:0000269|PubMed:11574907}.
CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC symporter transporter (TC 2.A.2) family. {ECO:0000305}.
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DR EMBL; AF360357; AAK81713.1; -; mRNA.
DR EMBL; AK029155; BAC26330.1; -; mRNA.
DR CCDS; CCDS27382.1; -.
DR RefSeq; NP_444307.1; NM_053077.3.
DR AlphaFoldDB; P58355; -.
DR STRING; 10090.ENSMUSP00000022851; -.
DR TCDB; 2.A.2.4.14; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR GlyGen; P58355; 1 site.
DR iPTMnet; P58355; -.
DR PhosphoSitePlus; P58355; -.
DR PaxDb; P58355; -.
DR PRIDE; P58355; -.
DR Antibodypedia; 22757; 118 antibodies from 23 providers.
DR DNASU; 22293; -.
DR Ensembl; ENSMUST00000117100; ENSMUSP00000112408; ENSMUSG00000022243.
DR GeneID; 22293; -.
DR KEGG; mmu:22293; -.
DR UCSC; uc007vgx.1; mouse.
DR CTD; 51151; -.
DR MGI; MGI:2153040; Slc45a2.
DR VEuPathDB; HostDB:ENSMUSG00000022243; -.
DR eggNOG; KOG0637; Eukaryota.
DR GeneTree; ENSGT00950000182914; -.
DR HOGENOM; CLU_015081_2_0_1; -.
DR InParanoid; P58355; -.
DR OMA; INVSMEP; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; P58355; -.
DR TreeFam; TF325412; -.
DR Reactome; R-MMU-5662702; Melanin biosynthesis.
DR BioGRID-ORCS; 22293; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc45a2; mouse.
DR PRO; PR:P58355; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P58355; protein.
DR Bgee; ENSMUSG00000022243; Expressed in iris and 28 other tissues.
DR ExpressionAtlas; P58355; baseline and differential.
DR Genevisible; P58355; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IDA:MGI.
DR GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0015770; P:sucrose transport; IDA:MGI.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Albinism; Disease variant; Glycoprotein; Melanin biosynthesis; Membrane;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1..530
FT /note="Membrane-associated transporter protein"
FT /id="PRO_0000122518"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 275..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 153
FT /note="D -> N (in UW-dbr)"
FT /evidence="ECO:0000269|PubMed:11574907"
FT VARIANT 435
FT /note="S -> P (in UW-dbr)"
FT /evidence="ECO:0000269|PubMed:11574907"
SQ SEQUENCE 530 AA; 57961 MW; F4EDEAD07916D9FC CRC64;
MSGSNGPTDT HTYQSLAEDC PFGSVEQPKR STGRLVMHSM AMFGREFCYA VEAAYVTPVL
LSVGLPKSLY SMVWLLSPIL GFLLQPVVGS ASDHCRARWG RRRPYILTLA IMMLLGMALY
LNGDAVVSAL VANPRQKLIW AISITMVGVV LFDFSADFID GPIKAYLFDV CSHQDKEKGL
HYHALFTGFG GALGYILGAI DWVHLDLGRL LGTEFQVMFF FSALVLILCF ITHLCSIPEA
PLRDAATDPP SQQDPQGSSL SASGMHEYGS IEKVKNGGAD TEQPVQEWKN KKPSGQSQRT
MSMKSLLRAL VNMPSHYRCL CVSHLIGWTA FLSNMLFFTD FMGQIVYHGD PYGAHNSTEF
LIYERGVEVG CWGLCINSVF SSVYSYFQKA MVSYIGLKGL YFMGYLLFGL GTGFIGLFPN
VYSTLVLCSM FGVMSSTLYT VPFNLIAEYH REEEKEKGQE APGGPDNQGR GKGVDCAALT
CMVQLAQILV GGGLGFLVNM AGSVVVVVIT ASAVSLIGCC FVALFVRYVD
