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UPK3A_BOVIN
ID   UPK3A_BOVIN             Reviewed;         287 AA.
AC   P38574;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Uroplakin-3a;
DE            Short=UP3a;
DE   AltName: Full=Uroplakin III;
DE            Short=UPIII;
DE   Flags: Precursor;
GN   Name=UPK3A; Synonyms=UPK3;
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 19-45; 174-181 AND
RP   209-235.
RC   TISSUE=Urinary bladder urothelium;
RX   PubMed=8270634; DOI=10.1242/jcs.106.1.31;
RA   Wu X.-R., Sun T.-T.;
RT   "Molecular cloning of a 47 kDa tissue-specific and differentiation-
RT   dependent urothelial cell surface glycoprotein.";
RL   J. Cell Sci. 106:31-43(1993).
RN   [2]
RP   INTERACTION WITH UPK1B, AND SUBCELLULAR LOCATION.
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 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.
CC   -!- SUBUNIT: Heterodimer with uroplakin-1B (UPK1B).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12475947}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:12475947}. Note=Heterodimer formation with UPK1B is
CC       a prerequisite to exit out of the endoplasmic reticulum (ER).
CC   -!- TISSUE SPECIFICITY: Bladder epithelium.
CC   -!- SIMILARITY: Belongs to the uroplakin-3 family. {ECO:0000305}.
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DR   EMBL; L19542; AAC37309.1; -; mRNA.
DR   PIR; I45986; I45986.
DR   RefSeq; NP_777134.1; NM_174709.3.
DR   AlphaFoldDB; P38574; -.
DR   STRING; 9913.ENSBTAP00000013081; -.
DR   PaxDb; P38574; -.
DR   Ensembl; ENSBTAT00000013081; ENSBTAP00000013081; ENSBTAG00000009913.
DR   GeneID; 100336102; -.
DR   KEGG; bta:100336102; -.
DR   CTD; 7380; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009913; -.
DR   VGNC; VGNC:36687; UPK3A.
DR   eggNOG; ENOG502S14V; Eukaryota.
DR   GeneTree; ENSGT00940000153392; -.
DR   HOGENOM; CLU_082608_1_0_1; -.
DR   InParanoid; P38574; -.
DR   OMA; EKPFCVF; -.
DR   OrthoDB; 1269506at2759; -.
DR   TreeFam; TF336628; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000009913; Expressed in urethra and 15 other tissues.
DR   GO; GO:0120001; C:apical plasma membrane urothelial plaque; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0015840; P:urea transport; IBA:GO_Central.
DR   GO; GO:0060157; P:urinary bladder development; IEA:Ensembl.
DR   GO; GO:0006833; P:water transport; IBA:GO_Central.
DR   InterPro; IPR024831; Uroplakin-3.
DR   InterPro; IPR024825; Uroplakin-3a.
DR   PANTHER; PTHR15446; PTHR15446; 1.
DR   PANTHER; PTHR15446:SF17; PTHR15446:SF17; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8270634"
FT   CHAIN           19..287
FT                   /note="Uroplakin-3a"
FT                   /id="PRO_0000022636"
FT   TOPO_DOM        19..207
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..287
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          243..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   287 AA;  30757 MW;  177185A017E233B5 CRC64;
     MPPLWVVLAL GCLRLGSGVN LQPQLASVTF ATNNPTLTTV ALEKPLCMFD SSAALHGTYE
     VYLYVLVDSA SFRNASVQDS TKTPLSSTFQ QTQGGRTGPY KAAAFDLTPC SDSPSLDAVR
     DVSRASEILN AYLIRVGTNG TCLLDPNFQG LCNPPLSAAT EYRFKYVLVN MSSGLVQDQT
     LWSDPIRTDR LTLYSAIDTW PGRRSGGMIV ITSILGSLPF FLLIGFAGAI VLSLVDRGDA
     DGATSHDSQI TQEAVPKSLG TSEPSYTSVN RGPSLDRAEV YASKLQD
 
 
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