ID   UPK1A_BOVIN             Reviewed;         258 AA.
AC   P38572;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Uroplakin-1a;
DE            Short=UP1a;
DE   AltName: Full=Uroplakin Ia;
DE            Short=UPIa;
GN   Name=UPK1A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Urinary bladder urothelium;
RX   PubMed=8138569; DOI=10.1083/jcb.125.1.171;
RA   Yu J., Lin J.-H., Wu X.-R., Sun T.-T.;
RT   "Uroplakins Ia and Ib, two major differentiation products of bladder
RT   epithelium, belong to a family of four transmembrane domain (4TM)
RT   proteins.";
RL   J. Cell Biol. 125:171-182(1994).
RN   [2]
RP   INTERACTION WITH UPK2.
RX   PubMed=12475947; DOI=10.1091/mbc.e02-04-0211;
RA   Tu L., Sun T.-T., Kreibich G.;
RT   "Specific heterodimer formation is a prerequisite for uroplakins to exit
RT   from the endoplasmic reticulum.";
RL   Mol. Biol. Cell 13:4221-4230(2002).
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.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with uroplakin-2
CC       (UPK2). {ECO:0000269|PubMed:12475947}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Bladder epithelium.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC   -!- PTM: N-glycosylated with high-mannose oligosaccharides.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z29475; CAA82613.1; -; mRNA.
DR   PIR; I46080; I46080.
DR   RefSeq; NP_788784.1; NM_176611.2.
DR   AlphaFoldDB; P38572; -.
DR   STRING; 9913.ENSBTAP00000027372; -.
DR   PaxDb; P38572; -.
DR   GeneID; 282112; -.
DR   KEGG; bta:282112; -.
DR   CTD; 11045; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; P38572; -.
DR   OrthoDB; 944403at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0120001; C:apical plasma membrane urothelial plaque; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA: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; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IDA: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   Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..258
FT                   /note="Uroplakin-1a"
FT                   /id="PRO_0000219285"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  28902 MW;  6E7FE3A981DE1BFC CRC64;
     MASAAAATTE KGSPVVVGLL VMGNIIILLS GLALFAETVW VTADQYRIYP LMGVSGKDDV
     FAGAWIAIFC GFSFFVVASF GVGAALCRRR SMILTYLILM LIIYIFECAS CITSYTHRDY
     MVSNPSLITK QMLTFYSADS NQGRELTRLW DRIMIEQECC GTSGPMDWVN FTSAFRATTP
     EVVFPWPPLC CRRTGNFIPV NEEGCRLGHL DYLFTKGCFE HIGHAIDSYT WGISWFGFAI
     LMWTLPVMLI AMYFYTTL