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UPK2_MOUSE
ID   UPK2_MOUSE              Reviewed;         184 AA.
AC   P38575;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Uroplakin-2;
DE            Short=UP2;
DE   AltName: Full=Uroplakin II;
DE            Short=UPII;
DE   Flags: Precursor;
GN   Name=Upk2;
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].
RX   PubMed=8175808; DOI=10.1016/s0021-9258(17)36889-8;
RA   Wu X.-R., Lin J.-H., Walz T., Haener M., Yu J., Aebi U., Sun T.-T.;
RT   "Mammalian uroplakins. A group of highly conserved urothelial
RT   differentiation-related membrane proteins.";
RL   J. Biol. Chem. 269:13716-13724(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=7846036; DOI=10.1073/pnas.92.3.679;
RA   Lin J.-H., Zhao H., Sun T.-T.;
RT   "A tissue-specific promoter that can drive a foreign gene to express in the
RT   suprabasal urothelial cells of transgenic mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:679-683(1995).
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 regulating the assembly
CC       of the AUM.
CC   -!- SUBUNIT: Interacts with uroplakin-1a (UPK1A). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A
CC       is a prerequisite to exit out of the endoplasmic reticulum (ER).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uroplakin-2 family. {ECO:0000305}.
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DR   EMBL; U08030; AAA19602.1; -; mRNA.
DR   EMBL; U14421; AAC52158.1; -; Genomic_DNA.
DR   CCDS; CCDS23112.1; -.
DR   PIR; A55603; A54135.
DR   AlphaFoldDB; P38575; -.
DR   STRING; 10090.ENSMUSP00000040481; -.
DR   GlyGen; P38575; 3 sites.
DR   PhosphoSitePlus; P38575; -.
DR   PaxDb; P38575; -.
DR   PRIDE; P38575; -.
DR   ProteomicsDB; 297870; -.
DR   MGI; MGI:98913; Upk2.
DR   eggNOG; KOG2294; Eukaryota.
DR   InParanoid; P38575; -.
DR   PhylomeDB; P38575; -.
DR   PRO; PR:P38575; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P38575; protein.
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:0030855; P:epithelial cell differentiation; ISO:MGI.
DR   CDD; cd09967; UP_II; 1.
DR   InterPro; IPR009952; Uroplakin-2.
DR   PANTHER; PTHR17573; PTHR17573; 1.
DR   Pfam; PF07353; Uroplakin_II; 1.
DR   PIRSF; PIRSF016439; Uroplakin_II; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cleavage on pair of basic residues; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..84
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022632"
FT   CHAIN           85..184
FT                   /note="Uroplakin-2"
FT                   /id="PRO_0000022633"
FT   TOPO_DOM        85..155
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   184 AA;  19572 MW;  E15E00C1EB1A7253 CRC64;
     MASTLPVQTL PLILILLAVL APGTADFNIS SLSGLLSPAL TESLLIALPP CHLTGGNATL
     MVRRANDSKV VKSDFVVPPC RGRRELVSVV DSGSGYTVTR LSAYQVTNLT PGTKYYISYR
     VQKGTSTESS PETPMSTLPR KNMESIGLGM ARTGGMVVIT VLLSVAMFLL VVGLIVALHW
     DARK
 
 
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