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Adenomatous polyposis coli protein-related protein 1 (APC-related protein 1)

 APR1_CAEEL              Reviewed;        1188 AA.
Q21227; O62302;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
22-NOV-2017, entry version 128.
RecName: Full=Adenomatous polyposis coli protein-related protein 1;
Short=APC-related protein 1;
Name=apr-1 {ECO:0000312|EMBL:AAC47747.1,
ECO:0000312|WormBase:K04G2.8a}; ORFNames=K04G2.8;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC47747.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47747.1};
PubMed=9288750; DOI=10.1016/S0092-8674(00)80531-0;
Rocheleau C.E., Downs W.D., Lin R., Wittmann C., Bei Y., Cha Y.-H.,
Ali M., Priess J.R., Mello C.C.;
"Wnt signaling and an APC-related gene specify endoderm in early C.
elegans embryos.";
Cell 90:707-716(1997).
[2] {ECO:0000312|EMBL:CAB00045.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10766743;
Hoier E.F., Mohler W.A., Kim S.K., Hajnal A.;
"The Caenorhabditis elegans APC-related gene apr-1 is required for
epithelial cell migration and Hox gene expression.";
Genes Dev. 14:874-886(2000).
[4] {ECO:0000305}
INTERACTION WITH BAR-1 AND HMP-2.
PubMed=11560894;
Natarajan L., Witwer N.E., Eisenmann D.M.;
"The divergent Caenorhabditis elegans beta-catenin proteins BAR-1,
WRM-1 and HMP-2 make distinct protein interactions but retain
functional redundancy in vivo.";
Genetics 159:159-172(2001).
[5] {ECO:0000305}
FUNCTION.
PubMed=12023306; DOI=10.1101/gad.981602;
Gleason J.E., Korswagen H.C., Eisenmann D.M.;
"Activation of Wnt signaling bypasses the requirement for RTK/Ras
signaling during C. elegans vulval induction.";
Genes Dev. 16:1281-1290(2002).
[6] {ECO:0000305}
FUNCTION, AND INTERACTION WITH PRY-1.
PubMed=12023307; DOI=10.1101/gad.981802;
Korswagen H.C., Coudreuse D.Y.M., Betist M.C., van de Water S.,
Zivkovic D., Clevers H.C.;
"The axin-like protein PRY-1 is a negative regulator of a canonical
Wnt pathway in C. elegans.";
Genes Dev. 16:1291-1302(2002).
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17276345; DOI=10.1016/j.devcel.2007.01.004;
Mizumoto K., Sawa H.;
"Cortical beta-catenin and APC regulate asymmetric nuclear beta-
catenin localization during asymmetric cell division in C. elegans.";
Dev. Cell 12:287-299(2007).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20805471; DOI=10.1073/pnas.1006600107;
Putzke A.P., Rothman J.H.;
"Repression of Wnt signaling by a Fer-type nonreceptor tyrosine
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 107:16154-16159(2010).
-!- FUNCTION: Has a role in endoderm cell specification and pharyngeal
development (PubMed:9288750). Required for the migration of
epithelial cells, organization of the anterior seam cells and ceh-
13 expression during embryo morphogenesis. Prevents
hyperactivation of the Wnt signaling pathway during endoderm
development, probably by preventing hmp-2 nuclear translocation
(PubMed:20805471). During larval development, apr-1 is required
for expression of lin-39 in P3-8.p (PubMed:10766743). Shown to
negatively regulate Wnt signaling in vulval precursor cells
(PubMed:12023306). Has a role in cell division by establishing the
polarity of the mother cell which forms the asymmetries of the
daughter nuclei (PubMed:17276345). Thought to regulate export of
wrm-1 from the nucleus possibly as part of a complex involving
pry-1 (PubMed:12023307). {ECO:0000269|PubMed:10766743,
ECO:0000269|PubMed:12023306, ECO:0000269|PubMed:12023307,
ECO:0000269|PubMed:17276345, ECO:0000269|PubMed:20805471,
ECO:0000269|PubMed:9288750}.
-!- SUBUNIT: Interacts (via N-terminus) with bar-1 and hmp-2; the
interaction with hmp-2 is relatively weak. Interacts (via C-
terminus) with pry-1 (via N-terminus). Probably associates with
bar-1, gsk-3, pry-1 in a complex. {ECO:0000269|PubMed:11560894,
ECO:0000269|PubMed:12023307}.
-!- SUBCELLULAR LOCATION: Cell junction, adherens junction
{ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}.
Cytoplasm {ECO:0000269|PubMed:10766743,
ECO:0000269|PubMed:17276345}. Nucleus
{ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}.
Note=Found in clusters near the ends of microtubules that extend
into regions of actively migrating plasma membranes. Shuttles
between the cytoplasm and nucleus. {ECO:0000269|PubMed:10766743,
ECO:0000269|PubMed:17276345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b {ECO:0000269|PubMed:9851916};
IsoId=Q21227-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=a {ECO:0000269|PubMed:9288750};
IsoId=Q21227-2; Sequence=VSP_052859;
-!- TISSUE SPECIFICITY: During the L1 stage, expressed in vulval
precursor cells (P3-8.p), seam cells and excretory cells.
{ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}.
-!- DISRUPTION PHENOTYPE: Worms exhibit lack of endoderm, excessive
pharyngeal tissue and premature division of the E daughter
blastomeres during embryogenesis. Two-thirds arrest during
embryogenesis and the remaining third during the L1 stage
(PubMed:9288750). RNAi-mediated knockdown causes partial nuclear
re-localization of hmp-2 in the embryonic epidermis and the
production of supernumerary gut nuclei probably resulting from
epithelial cell hyperproliferation (PubMed:20805471).
{ECO:0000269|PubMed:20805471, ECO:0000269|PubMed:9288750}.
-!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
family. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AF013950; AAC47747.1; -; mRNA.
EMBL; Z75712; CAB00045.1; -; Genomic_DNA.
EMBL; Z75712; CAB00048.1; -; Genomic_DNA.
PIR; T23327; T23327.
PIR; T23330; T23330.
RefSeq; NP_001021547.1; NM_001026376.4. [Q21227-1]
RefSeq; NP_492217.2; NM_059816.4. [Q21227-2]
UniGene; Cel.16875; -.
ProteinModelPortal; Q21227; -.
SMR; Q21227; -.
BioGrid; 38025; 7.
DIP; DIP-41257N; -.
IntAct; Q21227; 19.
MINT; MINT-214629; -.
STRING; 6239.K04G2.8b; -.
PaxDb; Q21227; -.
PeptideAtlas; Q21227; -.
EnsemblMetazoa; K04G2.8b; K04G2.8b; WBGene00000156. [Q21227-1]
GeneID; 172591; -.
KEGG; cel:CELE_K04G2.8; -.
UCSC; K04G2.8b; c. elegans. [Q21227-1]
CTD; 172591; -.
WormBase; K04G2.8a; CE06102; WBGene00000156; apr-1. [Q21227-2]
WormBase; K04G2.8b; CE18016; WBGene00000156; apr-1. [Q21227-1]
eggNOG; KOG2122; Eukaryota.
eggNOG; ENOG410XR2V; LUCA.
GeneTree; ENSGT00530000063749; -.
HOGENOM; HOG000034014; -.
InParanoid; Q21227; -.
OMA; GHSVENK; -.
OrthoDB; EOG091G00D4; -.
Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
SignaLink; Q21227; -.
PRO; PR:Q21227; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00000156; -.
ExpressionAtlas; Q21227; baseline.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0008013; F:beta-catenin binding; IPI:WormBase.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0001708; P:cell fate specification; IMP:WormBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
GO; GO:0007492; P:endoderm development; IMP:UniProtKB.
GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; IMP:UniProtKB.
GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:2000057; P:negative regulation of Wnt signaling pathway involved in digestive tract morphogenesis; IGI:UniProtKB.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:WormBase.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:WormBase.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
GO; GO:0016476; P:regulation of embryonic cell shape; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0040025; P:vulval development; IMP:WormBase.
GO; GO:0044333; P:Wnt signaling pathway involved in digestive tract morphogenesis; IMP:UniProtKB.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR026818; Apc_fam.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
PANTHER; PTHR12607; PTHR12607; 5.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Cell junction;
Complete proteome; Cytoplasm; Developmental protein; Nucleus;
Protein transport; Reference proteome; Transport;
Wnt signaling pathway.
CHAIN 1 1188 Adenomatous polyposis coli protein-
related protein 1.
/FTId=PRO_0000347250.
REPEAT 314 358 ARM. {ECO:0000255}.
REGION 1 486 Required for interaction with bar-1 and
hmp-2. {ECO:0000269|PubMed:11560894}.
REGION 600 1188 Required for interaction with pry-1.
{ECO:0000269|PubMed:12023307}.
COMPBIAS 491 589 Gln-rich. {ECO:0000255}.
COMPBIAS 953 996 Asp-rich. {ECO:0000255}.
VAR_SEQ 552 553 Missing (in isoform a).
{ECO:0000303|PubMed:9288750}.
/FTId=VSP_052859.
SEQUENCE 1188 AA; 131990 MW; F3CDA53B5D3527A0 CRC64;
MSSSSSDENE TTIHRTGSNT GGSGIYSQPR AGSSKRTSNV RHDVSDVDDE EEHYARFRED
TAIEVDDAIT VLLSSLHFEH KRDIVPTDED DNKLRELHEK IFALITSESD VNRKRRLKKA
LPASNCVREQ VYYLRRKPST PPASYYHRLN AALHTIVKES FGEEYRKVAT VLGLVEALAE
VLILEVHTFG INETNPGEHR NIRKLIANAL TNLTYGQIHS KRRLCSYDGF IRCVVRIVIE
SPNITQVYAG LIRNLSWNAD SGMSEALQPT VHALSIAAVH AHTHRFDVTA TLSALWNLAG
HSVENKRTIC DTPNCLKVLA SLLSPDARFT SLVDSATGIL KYVSQYLANT STHLELRSLL
ITRMLTLLKS ASFTCVTNTL GAIANLIVKD PHMQQMIRQD MAAVQQLNVL RNSNRDDIRT
AVKSVLNTLN QPCSHRYGDM SHSVGGGATG MQMLSEPQLQ MQTSHHAYHG TASPRLLSLR
ATRASPGKYI QPQAQQQLIQ TPQVDQRSSS LPRHFAVQRN GFVMAQSYNQ QMDQHQQQQM
IYQLQQQQQI MFQTEDQAQM EHHQQIMYLQ QQQQQFHQIQ QQQQMQKAQE ADPVPPTDDD
LDIPTSTVMG TRSNSERSLG SMNPGSVMTN WNSSLDTAAN SSRALSPVSY NDIPASPTMC
AQVFNLPKST ESEHHQLTSQ QQNTTHYSSG SANTMTRSDG ATTVPMDNII TPTYAILNPI
LVHEQTPNGT VPRKTSEELD SPDDVLPGPS LEEEEGDYAI IGGAAQKTDD ELLTRSIQSE
MPTSSSTPKM KVSPRLNGFF SPTQKTTSSP AWSHPDTSPI PKSSSHRTQP NRRQDASDAD
RLLMESIMSE MPKSRIISPR LAGTQQYLEP EPERRSHSKN EEADRRDAFT ASHEPSDHNG
IDVARGSDWS PQQQLHRMES LESQASSEDS FGLTAEEPNS STSGAAANTM RFDDEIDASL
PMDCVDDDDY DYTYDHFEDY EDEEDPDATQ FDDGVDAQLT IDCSMISSGS GSSQRNETTT
TSRDSKALAT STPKGSASSL PGVRQATRVS TNGKSRLPVP KTNGSLVDKN PKPIIASRRP
RLPPKPTLLK DKHYPEEDSI ENQTRDDTIY VNAPVVEAEQ ERIYMNALKQ QKNIEQSPSI
GNGSPIAKSA IVTPYNYQKP PFTGRNNGEM SNEKSVTPNP KQMLVTIV


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