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UPK2_BOVIN
ID   UPK2_BOVIN              Reviewed;         185 AA.
AC   Q08537;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Uroplakin-2;
DE            Short=UP2;
DE   AltName: Full=Uroplakin II;
DE            Short=UPII;
DE   Flags: Precursor;
GN   Name=UPK2;
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=7507484; DOI=10.1016/s0021-9258(17)42095-3;
RA   Lin J.-H., Wu X.-R., Kreibich G., Sun T.-T.;
RT   "Precursor sequence, processing, and urothelium-specific expression of a
RT   major 15-kDa protein subunit of asymmetric unit membrane.";
RL   J. Biol. Chem. 269:1775-1784(1994).
RN   [2]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH UPK1A.
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 regulating the assembly
CC       of the AUM.
CC   -!- SUBUNIT: Interacts with uroplakin-1a (UPK1A).
CC       {ECO:0000269|PubMed:12475947}.
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:0000269|PubMed:12475947}.
CC   -!- TISSUE SPECIFICITY: Bladder epithelium.
CC   -!- SIMILARITY: Belongs to the uroplakin-2 family. {ECO:0000305}.
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DR   EMBL; L20633; AAC37317.1; -; mRNA.
DR   PIR; A49713; A49713.
DR   RefSeq; NP_776639.1; NM_174214.2.
DR   RefSeq; XP_010810719.1; XM_010812417.2.
DR   AlphaFoldDB; Q08537; -.
DR   STRING; 9913.ENSBTAP00000016947; -.
DR   PaxDb; Q08537; -.
DR   Ensembl; ENSBTAT00000016947; ENSBTAP00000016947; ENSBTAG00000012750.
DR   GeneID; 281569; -.
DR   KEGG; bta:281569; -.
DR   CTD; 7379; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012750; -.
DR   VGNC; VGNC:36686; UPK2.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00390000006115; -.
DR   HOGENOM; CLU_126065_0_0_1; -.
DR   InParanoid; Q08537; -.
DR   OMA; PRRNMES; -.
DR   OrthoDB; 1415812at2759; -.
DR   TreeFam; TF337797; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000012750; Expressed in urethra and 28 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
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: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; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cell membrane; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..85
FT                   /id="PRO_0000022628"
FT   CHAIN           86..185
FT                   /note="Uroplakin-2"
FT                   /id="PRO_0000022629"
FT   TOPO_DOM        86..156
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   185 AA;  19619 MW;  CD8BA31D57489173 CRC64;
     MASPWPVWTL SWILILLAVL VPGAAADFNI SSLSGLLSPV MTESLLVALP PCHLTGGNAT
     LTVRRANDSK VVRSSFVVPP CRGRRELVSV VDSGSGFTVT RLSAYQVTNL APGTKYYISY
     LVTKGASTES SREIPMSTFP RRKAESIGLA MARTGGMVVI TVLLSVAMFL LVLGLIIALA
     LGARK
 
 
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