UPK1B_BOVIN
ID UPK1B_BOVIN Reviewed; 260 AA.
AC P38573; Q1LZG4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Uroplakin-1b;
DE Short=UP1b;
DE AltName: Full=Uroplakin Ib;
DE Short=UPIb;
GN Name=UPK1B;
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 PROTEIN SEQUENCE OF 2-21.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH UPK3B.
RC TISSUE=Urinary bladder urothelium;
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 [4]
RP INTERACTION WITH UPK3A.
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: Heterodimer with uroplakin-3A (UPK3A) or uroplakin-3B (UPK3B).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Bladder epithelium.
CC -!- PTM: N-glycosylated with high-mannose oligosaccharides.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; Z29378; CAA82569.1; -; mRNA.
DR EMBL; BC116014; AAI16015.1; -; mRNA.
DR PIR; I46081; I46081.
DR RefSeq; NP_776907.2; NM_174482.2.
DR RefSeq; XP_005201318.1; XM_005201261.3.
DR RefSeq; XP_010799373.1; XM_010801071.2.
DR AlphaFoldDB; P38573; -.
DR SMR; P38573; -.
DR STRING; 9913.ENSBTAP00000011866; -.
DR PaxDb; P38573; -.
DR GeneID; 282113; -.
DR KEGG; bta:282113; -.
DR CTD; 7348; -.
DR eggNOG; KOG3882; Eukaryota.
DR HOGENOM; CLU_088971_1_0_1; -.
DR InParanoid; P38573; -.
DR OrthoDB; 944403at2759; -.
DR TreeFam; TF335659; -.
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:0034394; P:protein localization to cell surface; IPI: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; IPR034766; Uroplakin-1b.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR PANTHER; PTHR19282:SF24; PTHR19282:SF24; 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; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8138569"
FT CHAIN 2..260
FT /note="Uroplakin-1b"
FT /id="PRO_0000219288"
FT TOPO_DOM 2..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 64
FT /note="F -> S (in Ref. 1; CAA82569)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="Q -> H (in Ref. 1; CAA82569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29730 MW; DFE18874657B1E60 CRC64;
MAKDDSTVRC FQGLLIFGNV IIGMCSIALM AECIFFVSDQ NSLYPLLEAT NNDDIYAAAW
IGMFVGICLF CLSVLGIVGI MKSNRKILLV YFILMFIVYA FEVASCITAA TQRDFFTPNL
FLKQMLERYQ NNSPPNNDDQ WKNNGVTKTW DRLMLQDNCC GVNGPSDWQK YTSAFRTENS
DADYPWPRQC CVMNSLKEPL NLDACKLGVP GYYHSQGCYE LISGPMNRHA WGVAWFGFAI
LCWTFWVLLG TMFYWSRIDY