UPK1A_MOUSE
ID UPK1A_MOUSE Reviewed; 257 AA.
AC Q9D132;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Uroplakin-1a;
DE Short=UP1a;
DE AltName: Full=Uroplakin Ia;
DE Short=UPIa;
DE Short=UPKa;
GN Name=Upk1a;
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], AND INTERACTION WITH E.COLI FIMH.
RC TISSUE=Urinary bladder;
RX PubMed=11739641; DOI=10.1242/jcs.114.22.4095;
RA Zhou G., Mo W.J., Sebbel P., Min G., Neubert T.A., Glockshuber R., Wu X.R.,
RA Sun T.T., Kong X.P.;
RT "Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia
RT coli: evidence from in vitro FimH binding.";
RL J. Cell Sci. 114:4095-4103(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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: Component of the asymmetric unit membrane (AUM); a highly
CC specialized biomembrane elaborated by terminally differentiated
CC urothelial cells. May play an important role in normal bladder
CC epithelial physiology, possibly in regulating membrane permeability of
CC superficial umbrella cells or in stabilizing the apical membrane
CC through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with uroplakin-2 (UPK2)
CC (By similarity). Binds to uropathogenic E.coli fimH. {ECO:0000250,
CC ECO:0000269|PubMed:11739641}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AF262335; AAM08129.1; -; mRNA.
DR EMBL; AK004014; BAB23125.1; -; mRNA.
DR CCDS; CCDS21103.1; -.
DR RefSeq; NP_081091.1; NM_026815.2.
DR AlphaFoldDB; Q9D132; -.
DR SMR; Q9D132; -.
DR STRING; 10090.ENSMUSP00000006476; -.
DR GlyGen; Q9D132; 1 site.
DR PhosphoSitePlus; Q9D132; -.
DR PaxDb; Q9D132; -.
DR PRIDE; Q9D132; -.
DR ProteomicsDB; 297868; -.
DR Antibodypedia; 54114; 140 antibodies from 26 providers.
DR Ensembl; ENSMUST00000006476; ENSMUSP00000006476; ENSMUSG00000006313.
DR GeneID; 109637; -.
DR KEGG; mmu:109637; -.
DR UCSC; uc009gfk.2; mouse.
DR CTD; 11045; -.
DR MGI; MGI:98911; Upk1a.
DR VEuPathDB; HostDB:ENSMUSG00000006313; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000160881; -.
DR HOGENOM; CLU_088971_1_0_1; -.
DR InParanoid; Q9D132; -.
DR OMA; HVDYLFT; -.
DR OrthoDB; 944403at2759; -.
DR PhylomeDB; Q9D132; -.
DR TreeFam; TF335659; -.
DR BioGRID-ORCS; 109637; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Upk1a; mouse.
DR PRO; PR:Q9D132; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D132; protein.
DR Bgee; ENSMUSG00000006313; Expressed in urinary bladder urothelium and 96 other tissues.
DR ExpressionAtlas; Q9D132; baseline and differential.
DR Genevisible; Q9D132; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0120001; C:apical plasma membrane urothelial plaque; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR InterPro; IPR034765; Uroplakin-1a.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR PANTHER; PTHR19282:SF25; PTHR19282:SF25; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..257
FT /note="Uroplakin-1a"
FT /id="PRO_0000219287"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28854 MW; 882215F25A5848ED CRC64;
MASAATEGEK GSPVVVGLLV VGNIIILLSG LALFAETVWV TADQYRVYPL MGVSGKDDVF
AGAWIAIFCG FSFFVVASFG VGAALCRRRY MILTYLLLML IVYIFECASC ITSYTHRDYM
VSNPSLITKQ MLTYYSADTD QGQELTRLWD RIMIEQECCG TSGPMDWVNY TSAFRAATPE
VVFPWPPLCC RRTGNFIPIN EDGCRVGHMD YLFTKGCFEH IGHAIDSYTW GISWFGFAIL
MWTLPVMLIA MYFYTTL
