ID UPK3B_HUMAN Reviewed; 320 AA. AC Q9BT76; A6NHH5; A8K231; A8MZA8; B3KPU5; Q75MM5; Q86W06; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 158. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH UPK1B, SUBCELLULAR RP LOCATION, AND VARIANT ARG-319. 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] (ISOFORMS 1 AND 2), AND VARIANT RP ARG-319. RC TISSUE=Placenta, and Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-319. RC TISSUE=Uterus; 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=3; CC Name=1; CC IsoId=Q9BT76-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BT76-2; Sequence=VSP_037327; CC Name=3; CC IsoId=Q9BT76-3; Sequence=VSP_037327, VSP_054295; CC -!- SIMILARITY: Belongs to the uroplakin-3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO89507.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAS07526.1; Type=Erroneous gene model prediction; Evidence={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; AY233462; AAO89507.1; ALT_FRAME; mRNA. DR EMBL; AK056760; BAG51807.1; -; mRNA. DR EMBL; AK290096; BAF82785.1; -; mRNA. DR EMBL; AC004980; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007003; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114737; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007078; AAS07526.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC004304; AAH04304.1; -; mRNA. DR CCDS; CCDS87512.1; -. [Q9BT76-3] DR RefSeq; NP_001334613.1; NM_001347684.1. [Q9BT76-3] DR RefSeq; NP_085047.1; NM_030570.3. DR RefSeq; NP_872624.1; NM_182683.2. DR RefSeq; NP_872625.1; NM_182684.2. DR RefSeq; XP_005250669.1; XM_005250612.3. DR RefSeq; XP_006716203.1; XM_006716140.3. DR RefSeq; XP_006716204.1; XM_006716141.3. DR AlphaFoldDB; Q9BT76; -. DR BioGRID; 123295; 16. DR IntAct; Q9BT76; 5. DR MINT; Q9BT76; -. DR TCDB; 8.A.90.2.2; the uroplakin 2/3 (upk2/3) family. DR GlyCosmos; Q9BT76; 1 site, No reported glycans. DR GlyGen; Q9BT76; 1 site. DR iPTMnet; Q9BT76; -. DR PhosphoSitePlus; Q9BT76; -. DR BioMuta; UPK3B; -. DR MassIVE; Q9BT76; -. DR PaxDb; 9606-ENSP00000257632; -. DR PeptideAtlas; Q9BT76; -. DR ProteomicsDB; 1200; -. DR ProteomicsDB; 78956; -. [Q9BT76-1] DR ProteomicsDB; 78957; -. [Q9BT76-2] DR Antibodypedia; 34816; 124 antibodies from 22 providers. DR DNASU; 80761; -. DR Ensembl; ENST00000257632.9; ENSP00000257632.5; ENSG00000243566.7. [Q9BT76-1] DR Ensembl; ENST00000334348.8; ENSP00000334938.3; ENSG00000243566.7. [Q9BT76-3] DR Ensembl; ENST00000394849.1; ENSP00000378319.1; ENSG00000243566.7. [Q9BT76-2] DR Ensembl; ENST00000448265.7; ENSP00000441284.2; ENSG00000276184.4. DR Ensembl; ENST00000615976.2; ENSP00000479568.1; ENSG00000276184.4. DR GeneID; 105375355; -. DR KEGG; hsa:105375355; -. DR MANE-Select; ENST00000334348.8; ENSP00000334938.3; NM_001347684.2; NP_001334613.1. [Q9BT76-3] DR UCSC; uc033ayx.2; human. [Q9BT76-1] DR AGR; HGNC:21444; -. DR CTD; 105375355; -. DR DisGeNET; 105375355; -. DR GeneCards; UPK3B; -. DR HGNC; HGNC:21444; UPK3B. DR HPA; ENSG00000243566; Group enriched (adipose tissue, esophagus, lung, urinary bladder). DR MIM; 611887; gene. DR neXtProt; NX_Q9BT76; -. DR OpenTargets; ENSG00000243566; -. DR PharmGKB; PA134952181; -. DR VEuPathDB; HostDB:ENSG00000243566; -. DR eggNOG; ENOG502RZJD; Eukaryota. DR GeneTree; ENSGT00940000153392; -. DR HOGENOM; CLU_082608_0_0_1; -. DR InParanoid; Q9BT76; -. DR OMA; HFSSLWW; -. DR OrthoDB; 5318376at2759; -. DR PhylomeDB; Q9BT76; -. DR TreeFam; TF336628; -. DR PathwayCommons; Q9BT76; -. DR SignaLink; Q9BT76; -. DR BioGRID-ORCS; 105375355; 15 hits in 1047 CRISPR screens. DR GenomeRNAi; 105375355; -. DR Pharos; Q9BT76; Tbio. DR PRO; PR:Q9BT76; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9BT76; Protein. DR Bgee; ENSG00000243566; Expressed in lower esophagus mucosa and 91 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB. DR InterPro; IPR024831; Uroplakin-3. DR PANTHER; PTHR15446; UROPLAKIN III; 1. DR PANTHER; PTHR15446:SF15; UROPLAKIN-3B; 1. DR Genevisible; Q9BT76; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Glycoprotein; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..320 FT /note="Uroplakin-3b" FT /id="PRO_0000022640" FT TOPO_DOM 30..240 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 241..266 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 267..320 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 273..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 29..83 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12446744, FT ECO:0000303|PubMed:14702039" FT /id="VSP_037327" FT VAR_SEQ 210..320 FT /note="EDPRIHRHLARAAKWQHDRHYLHPLFSGRPPTLGLLGSLYHALLQPVVAGGG FT PGAAADRLLHGQALHDPPHPTQRGRHTAGGLQAWPGPPPQPQPLAWPLCMGLGEMGRWE FT -> VKFLLMDTRGSPRAETKWSDPITLHQGKTPGSIDTWPGRRSGSMIVITSILSSLAG FT LLLLAFLAASTMRFSSLWWPEEAPEQLRIGSFMGKRYMTHHIPPREAATLPVGCKPGLD FT PLPSLSP (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_054295" FT VARIANT 293 FT /note="Q -> R (in dbSNP:rs1636632)" FT /id="VAR_034561" FT VARIANT 319 FT /note="W -> R (in dbSNP:rs1799126)" FT /evidence="ECO:0000269|PubMed:12446744, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_047805" SQ SEQUENCE 320 AA; 33882 MW; 64A1FE268A8BB0EB CRC64; MGLPWGQPHL GLQMLLLALN CLRPSLSLGE WGSWMDASSQ TQGAGGPAGV IGPWAPAPLR LGEAAPGTPT PVSVAHLLSP VATELVPYTP QITAWDLEGK VTATTFSLEQ PRCVFDGLAS ASDTVWLVVA FSNASRGFQN PETLADIPAS PQLLTDGHYM TLPLSPDQLP CGDPMAGSGG APVLRVGHDH GCHQQPFCNA PLPGPGPYRE DPRIHRHLAR AAKWQHDRHY LHPLFSGRPP TLGLLGSLYH ALLQPVVAGG GPGAAADRLL HGQALHDPPH PTQRGRHTAG GLQAWPGPPP QPQPLAWPLC MGLGEMGRWE //