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Mucin-1 (MUC-1) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]

 MUC1_MESAU              Reviewed;         676 AA.
Q60528;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 83.
RecName: Full=Mucin-1;
Short=MUC-1;
AltName: CD_antigen=CD227;
Contains:
RecName: Full=Mucin-1 subunit alpha;
Short=MUC1-NT;
Short=MUC1-alpha;
Contains:
RecName: Full=Mucin-1 subunit beta;
Short=MUC1-beta;
AltName: Full=MUC1-CT;
Flags: Precursor;
Name=MUC1;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Tracheal epithelium;
PubMed=8703480; DOI=10.1165/ajrcmb.15.2.8703480;
Park H., Hyun S.W., Kim K.C.;
"Expression of MUC1 mucin gene by hamster tracheal surface epithelial
cells in primary culture.";
Am. J. Respir. Cell Mol. Biol. 15:237-244(1996).
-!- FUNCTION: The alpha subunit has cell adhesive properties. Can act
both as an adhesion and an anti-adhesion protein. May provide a
protective layer on epithelial cells against bacterial and enzyme
attack (By similarity). {ECO:0000250}.
-!- FUNCTION: The beta subunit contains a C-terminal domain which is
involved in cell signaling, through phosphorylations and protein-
protein interactions. Modulates signaling in ERK, Src and NF-
kappaB pathways. In activated T-cells, influences directly or
indirectly the Ras/MAPK pathway. Promotes tumor progression.
Regulates P53-mediated transcription and determines cell fate in
the genotoxic stress response. Binds, together with KLF4, the PE21
promoter element of P53 and represses P53 activity (By
similarity). {ECO:0000250}.
-!- SUBUNIT: The alpha subunit forms a tight, non-covalent
heterodimeric complex with the proteolytically-released beta-
subunit. Binds directly the SH2 domain of GRB2, and forms a
MUC1/GRB2/SOS1 complex involved in RAS signaling. The cytoplasmic
tail (MUC1CT) interacts with several proteins such as SRC, CTNNB1
and ERBs. Interaction with the SH2 domain of CSK decreases
interaction with GSK3B. Interacts with CTNNB1/beta-catenin and
JUP/gamma-catenin and promotes cell adhesion. Interaction with
JUP/gamma-catenin is induced by heregulin. Binds PRKCD, ERBB2,
ERBB3 and ERBB4. Heregulin (HRG) stimulates the interaction with
ERBB2 and, to a much lesser extent, the interaction with ERBB3 and
ERBB4. Interacts with P53 in response to DNA damage. Interacts
with KLF4. Interacts with estrogen receptor alpha/ESR1, through
its DNA-binding domain, and stimulates its transcription activity.
Binds ADAM17 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type I
membrane protein. Note=Exclusively located in the apical domain of
the plasma membrane of highly polarized epithelial cells. After
endocytosis, internalized and recycled to the cell membrane.
Located to microvilli and to the tips of long filopodial
protusions (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mucin-1 subunit beta: Cell membrane.
Cytoplasm. Nucleus. Note=On EGF and PDGFRB stimulation,
transported to the nucleus through interaction with CTNNB1, a
process which is stimulated by phosphorylation. On HRG
stimulation, colocalizes with JUP/gamma-catenin at the nucleus.
-!- PTM: Probably both N- and O-glycosylated (in repeat region).
-!- PTM: Proteolytic cleavage in the SEA domain occurs in the
endoplasmic reticulum by an autoproteolytic mechanism and requires
the full-length SEA domain as well as requiring a Ser, Thr or Cys
residue at the P + 1 site. Ectodomain shedding is mediated by
ADAM17 in uterine epithelial cells (By similarity). {ECO:0000250}.
-!- PTM: Dual palmitoylation on cysteine residues in the CQC motif is
required for recycling from endosomes back to the plasma membrane.
{ECO:0000250}.
-!- PTM: Phosphorylated on tyrosines and serine residues in the C-
terminal. Phosphorylation on tyrosines in the C-terminal increases
the nuclear location of MUC1 and beta-catenin. Phosphorylation by
PKC delta induces binding of MUC1 to beta-catenin/CTNNB1 and thus
decreases the formation of the beta-catenin/E-cadherin complex.
Src-mediated phosphorylation inhibits interaction with GSK3B.
Csk- or Src- or EGFR-mediated phosphorylation on Tyr-651 increases
binding to beta-catenin/CTNNB1. GSK3B-mediated phosphorylation on
Ser-649 decreases this interaction but restores the formation of
the beta-cadherin/E-cadherin complex. On T-cell receptor
activation, phosphorylated by LCK. PDGFR-mediated phosphorylation
increases nuclear colocalization of MUC1CT and CTNNB1 (By
similarity). {ECO:0000250}.
-!- CAUTION: O-glycosylation sites are annotated in first sequence
repeat only. Residues at similar position are probably
glycosylated in all repeats. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U36918; AAB53965.1; -; mRNA.
RefSeq; NP_001268584.1; NM_001281655.1.
ProteinModelPortal; Q60528; -.
SMR; Q60528; -.
GeneID; 101835702; -.
CTD; 4582; -.
HOVERGEN; HBG003075; -.
OrthoDB; EOG091G0P86; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
Gene3D; 3.30.70.960; -; 1.
InterPro; IPR000082; SEA_dom.
InterPro; IPR036364; SEA_dom_sf.
Pfam; PF01390; SEA; 1.
SMART; SM00200; SEA; 1.
SUPFAM; SSF82671; SSF82671; 1.
PROSITE; PS50024; SEA; 1.
2: Evidence at transcript level;
Autocatalytic cleavage; Cell membrane; Complete proteome; Cytoplasm;
Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 676 Mucin-1.
/FTId=PRO_0000019279.
CHAIN 26 520 Mucin-1 subunit alpha. {ECO:0000250}.
/FTId=PRO_0000317450.
CHAIN 521 676 Mucin-1 subunit beta. {ECO:0000250}.
/FTId=PRO_0000317451.
TOPO_DOM 26 582 Extracellular. {ECO:0000255}.
TRANSMEM 583 603 Helical. {ECO:0000255}.
TOPO_DOM 604 676 Cytoplasmic. {ECO:0000255}.
REPEAT 40 59 1.
REPEAT 60 79 2.
REPEAT 80 99 3.
REPEAT 100 119 4.
REPEAT 120 139 5.
REPEAT 140 159 6.
REPEAT 160 179 7.
REPEAT 180 199 8.
REPEAT 200 219 9.
REPEAT 220 239 10.
REPEAT 240 259 11.
REPEAT 260 279 12.
REPEAT 280 299 13.
DOMAIN 463 570 SEA. {ECO:0000255|PROSITE-
ProRule:PRU00188}.
REGION 40 314 13 X approximate tandem repeats of P-V-H-
S-G-S-S-A-P-P-T-S-S-A-V-N-S-A-T-T.
REGION 614 650 Interaction with P53. {ECO:0000250}.
REGION 645 652 Required for interaction with GSK3B.
{ECO:0000250}.
REGION 655 662 Required for interaction with beta- and
gamma-catenins. {ECO:0000250}.
MOTIF 625 628 Interaction with GRB2. {ECO:0000250}.
MOTIF 651 654 Interaction with SRC and ESR1.
{ECO:0000250}.
MOTIF 664 667 Required for interaction with AP1S2.
{ECO:0000250}.
SITE 520 521 Cleavage; by autolysis. {ECO:0000250}.
MOD_RES 625 625 Phosphotyrosine; by PDGFR.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 634 634 Phosphotyrosine.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 640 640 Phosphotyrosine; by PDGFR.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 646 646 Phosphothreonine; by PKC/PRKCD.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 649 649 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 651 651 Phosphotyrosine; by CSK, EGFR and SRC.
{ECO:0000250|UniProtKB:P15941}.
MOD_RES 664 664 Phosphotyrosine.
{ECO:0000250|UniProtKB:P15941}.
LIPID 606 606 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 608 608 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 43 43 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 45 45 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 46 46 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 50 50 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 51 51 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 52 52 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 56 56 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 58 58 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 59 59 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 676 AA; 67617 MW; 95F479B6EC5C3884 CRC64;
MTPGIRAPFL LTLLLALVTD PNSVALSQDT SSSSTLNTTP VHSGSSAPAT SSAVDSATTP
GHSGSSAPPT SSAVNSATTP GHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP
VHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPVT SSAVDSATTP
VHSGSSAPPT SSAVNSATTP VHSGSSAPVT SSAVNSATTP VHSGSSAPVT SSAVNSATTP
VHSGSSAPPT SSVVNSATTP VHSGSSAPPT SSAVNLATTP VHSGSSTPAT NSTTDSATTP
VPPGSSMQTT EAISGSANTP IHNGSLVPTT SSALVPTTSA AHSGASAMTN SSESDLATTP
IDSGTSISTT KAPATTPVHN GSLVPTTSSV LGSATTLIHN DTSTMATTTP VGNGTQSSVP
SRHPVTPTPP AVSSNSTIAL STYYSTALSP AFSSHAAPQV SVGVSFFLLS FHIWNHQFNS
SLEDPSSNYY QELKRNVSGL FLQVFSRAFL GISTIEFRSG SVVVDSTVIF REGAVNASEV
KSQLLQHEQE AEEYNLAISK INVGEMQFPS SAQSWPGVPG WGIALLVLVC ILVALAIVYL
IALAVCQCRR KNYGQLDIFP IQDSYHPMSE YPTYHTHGRY VPPGSTKRSP YEEVSAGNGS
SLSYTNPVVA TTSANL


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