UPK3B_MOUSE
ID UPK3B_MOUSE Reviewed; 275 AA.
AC Q80YF6; Q0VBK9; Q6P8J5; Q8BGL8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Uroplakin-3b;
DE Short=UP3b;
DE AltName: Full=Uroplakin IIIb;
DE Short=UPIIIb;
DE AltName: Full=p35;
DE Flags: Precursor;
GN Name=Upk3b;
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] (ISOFORM 1), INTERACTION WITH UPK1B, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12446744; DOI=10.1083/jcb.200204102;
RA Deng F.-M., Liang F.-X., Tu L., Resing K.A., Hu P., Supino M., Hu C.-C.A.,
RA Zhou G., Ding M., Kreibich G., Sun T.-T.;
RT "Uroplakin IIIb, a urothelial differentiation marker, dimerizes with
RT uroplakin Ib as an early step of urothelial plaque assembly.";
RL J. Cell Biol. 159:685-694(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Thymus;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart, Lung, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 AUM-cytoskeleton
CC interaction in terminally differentiated urothelial cells. It also
CC contributes to the formation of urothelial glycocalyx which may play an
CC important role in preventing bacterial adherence (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with uroplakin-1B (UPK1B).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1B
CC is a prerequisite to exit out of the endoplasmic reticulum (ER).
CC {ECO:0000269|PubMed:12446744}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YF6-2; Sequence=VSP_035890;
CC -!- TISSUE SPECIFICITY: Expression is urothelium-specific.
CC {ECO:0000269|PubMed:12446744}.
CC -!- SIMILARITY: Belongs to the uroplakin-3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61224.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY233463; AAO89508.1; -; mRNA.
DR EMBL; AK042067; BAC31149.1; -; mRNA.
DR EMBL; AK052525; BAC35025.1; -; mRNA.
DR EMBL; BC061224; AAH61224.1; ALT_SEQ; mRNA.
DR EMBL; BC120594; AAI20595.1; -; mRNA.
DR EMBL; BC137742; AAI37743.1; -; mRNA.
DR CCDS; CCDS19750.1; -. [Q80YF6-2]
DR RefSeq; NP_780518.1; NM_175309.4.
DR AlphaFoldDB; Q80YF6; -.
DR STRING; 10090.ENSMUSP00000062312; -.
DR GlyGen; Q80YF6; 1 site.
DR iPTMnet; Q80YF6; -.
DR PhosphoSitePlus; Q80YF6; -.
DR MaxQB; Q80YF6; -.
DR PaxDb; Q80YF6; -.
DR PRIDE; Q80YF6; -.
DR ProteomicsDB; 297872; -. [Q80YF6-1]
DR ProteomicsDB; 297873; -. [Q80YF6-2]
DR DNASU; 100647; -.
DR GeneID; 100647; -.
DR KEGG; mmu:100647; -.
DR UCSC; uc008zzq.1; mouse. [Q80YF6-2]
DR CTD; 105375355; -.
DR MGI; MGI:2140882; Upk3b.
DR eggNOG; ENOG502RZJD; Eukaryota.
DR InParanoid; Q80YF6; -.
DR OrthoDB; 1269506at2759; -.
DR PhylomeDB; Q80YF6; -.
DR TreeFam; TF336628; -.
DR BioGRID-ORCS; 100647; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q80YF6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80YF6; protein.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0046325; P:negative regulation of glucose import; IMP:CACAO.
DR InterPro; IPR024831; Uroplakin-3.
DR InterPro; IPR024828; Uroplakin-3b.
DR PANTHER; PTHR15446; PTHR15446; 1.
DR PANTHER; PTHR15446:SF15; PTHR15446:SF15; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..275
FT /note="Uroplakin-3b"
FT /id="PRO_0000022641"
FT TOPO_DOM 27..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 9..12
FT /note="PLRA -> HPPPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035890"
FT CONFLICT 125
FT /note="A -> V (in Ref. 2; BAC31149/BAC35025 and 3;
FT AAH61224/AAI37743/AAI20595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 30227 MW; 49C06E45E12E80A1 CRC64;
MVRTRWQPPL RALLLLVLVW LPQSLSLDLI AYVPQITAWD LEGKITATTF SLEQPRCVFD
EHVSTKDTIW LVVAFSNASR DFQNPQTAAK IPTFPQLLTD GHYMTLPLSL DQLPCEDLTG
GSGGAPVLRV GNDFGCYQRP YCNAPLPSQG PYSVKFLVMD AAGPPKAETK WSNPIYLHQG
KNPNSIDTWP GRRSGCMIVI TSILSALAGL LLLAFLAAST TRFSSLWWPE EAPEQLRIGS
FMGKRYMTHH IPPSEAATLP VGCEPGLDPL PSLSP
