ID   APR1_CAEBR              Reviewed;        1171 AA.
AC   A8X633;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=APC-related protein 1 {ECO:0000250|UniProtKB:Q21227};
GN   Name=apr-1 {ECO:0000312|EMBL:CAP28094.1}; ORFNames=CBG08224;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP28094.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP28094.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Has a role in endoderm cell specification and pharyngeal
CC       development. Required for the migration of epithelial cells,
CC       organization of the anterior seam cells and ceh-13 expression during
CC       embryo morphogenesis. Prevents hyperactivation of the Wnt signaling
CC       pathway during endoderm development, probably by preventing hmp-2
CC       nuclear translocation. During larval development, apr-1 is required for
CC       expression of lin-39 in P3-8.p. Shown to negatively regulate Wnt
CC       signaling in vulval precursor cells. Has a role in cell division by
CC       establishing the polarity of the mother cell which forms the
CC       asymmetries of the daughter nuclei. Thought to regulate export of wrm-1
CC       from the nucleus possibly as part of a complex involving pry-1.
CC       {ECO:0000250|UniProtKB:Q21227}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with bar-1 and hmp-2; the
CC       interaction with hmp-2 is relatively weak. Interacts (via C-terminus)
CC       with pry-1 (via N-terminus). Probably associates with bar-1, gsk-3,
CC       pry-1 in a complex (By similarity). {ECO:0000250|UniProtKB:Q21227}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:Q21227}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q21227}. Nucleus {ECO:0000250|UniProtKB:Q21227}.
CC       Note=Found in clusters near the ends of microtubules that extend into
CC       regions of actively migrating plasma membranes. Shuttles between the
CC       cytoplasm and nucleus (By similarity). {ECO:0000250|UniProtKB:Q21227}.
CC   -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC       {ECO:0000255}.
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DR   EMBL; HE601064; CAP28094.1; -; Genomic_DNA.
DR   RefSeq; XP_002639900.1; XM_002639854.1.
DR   AlphaFoldDB; A8X633; -.
DR   SMR; A8X633; -.
DR   STRING; 6238.CBG08224; -.
DR   GeneID; 8581894; -.
DR   KEGG; cbr:CBG_08224; -.
DR   CTD; 8581894; -.
DR   WormBase; CBG08224a; CBP45043; WBGene00030061; Cbr-apr-1.
DR   eggNOG; KOG2122; Eukaryota.
DR   HOGENOM; CLU_272401_0_0_1; -.
DR   InParanoid; A8X633; -.
DR   OMA; CVDDEDY; -.
DR   OrthoDB; 268832at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0008356; P:asymmetric cell division; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007492; P:endoderm development; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR026818; Apc_fam.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   PANTHER; PTHR12607; PTHR12607; 3.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell junction; Cytoplasm; Developmental protein;
KW   Nucleus; Protein transport; Reference proteome; Transport;
KW   Wnt signaling pathway.
FT   CHAIN           1..1171
FT                   /note="APC-related protein 1"
FT                   /id="PRO_0000347279"
FT   REPEAT          312..356
FT                   /note="ARM"
FT                   /evidence="ECO:0000255"
FT   REGION          1..481
FT                   /note="Required for interaction with bar-1 and hmp-2"
FT                   /evidence="ECO:0000250|UniProtKB:Q21227"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..1171
FT                   /note="Required for interaction with pry-1"
FT                   /evidence="ECO:0000250|UniProtKB:Q21227"
FT   REGION          662..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..878
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  130298 MW;  CB76A3EE17C54CA0 CRC64;
     MSSSSSDENE TTIHSSSNPG SSGIYSQLKA GSSKRPSVRH DVSDAEDDEE PYEGFRKDMN
     MEVDERITTL LSSLHFEHKR DVVTADEDDN KLRELHENIF SLITTEPDFH RRRRLKKALP
     ASNCIREQVY YLRRKPITPP DSYYHRLNAA LHTIVKESFG EEYRKVATVL GLVEALAEVL
     ILEVHAFGIP ETNAVEHRNI RKLIANALTN LTYGQILSKR RLCSYDGFIR CVVRIIIESP
     NITQVYAGLI RNLSWNADSG MSEALQPTVH ALSLAAVYAH THRFDVTAIL SALWNLAGHS
     VENKRTICET PNCLKVLANI LSPDARFTTL VDSASGILKY VSQYLATNSS HLELRSLLIT
     RMLTLLKSSS FTCVTNTLGA IAHLIAKDPH MQQLIRQDAA AVQQLNVLRN SNREDIRKAV
     KEVLNTLNQP CSHRYGDMSH SVGGASGMLS EPQLQMQTSH HGYHGTASPR LLSLRATRAS
     PGKYIHPSQQ QHMQVPAPDQ RSSSLPRHFA VQRNGFMMAQ SFNQQMDPHQ QQQQQQQQMI
     FQMQQQQMMI QTDDQQMRYL NQQQQQQQQQ HYQQQIQRNQ NVEPVLPVDD DLDIPTSTVM
     GTRSNSERSL GSMNPGSVMT TGGWNSTLDT AANSSRALSP VSFSDIPASP TMCAQVFNLP
     VHPEDNQMTT PPNHPSTQNT THYSSGSANT MTRSDGTTVP IDNLITPTYA TLNVTNNAAR
     KTSEDLESPD DILPGPSLEV EEEGDYAIIT GAEQKSDDDL LTRSIQEEMP TSSSTPKLKV
     SPRLNGFFSP SQKTTSSPAW SHPDTSPILK QTQRPKHHEM TTDSDRLLME SIMSEMPRSR
     VISPRLASGG QQYLDPEPDR SSHSKNEEAD RRDAIIASHE PSDQGMNVGR GSSPQQQQLH
     RMESLESQAS SEDSFGLNGY QEEHNTSSSA AHTMRIDKDD VVDASLPMDC VDDEDYDYTD
     DHFDDNYEED YEDSNATQFD EGIDPQLTID CSMISSGSGS SLQKAETTAG SRDSGALATS
     TPIGSVSSLP GVRRAKKVSI NGKTRLPVPK TNGSLVDRVR KPVIEASRPR LPPKPSLLKG
     KQYHEEDLIE NQTRDDTIYV NAPIVEAEQE RIYMNALKHS QGSPSVNGTP PKSAIVSPYN
     YQKPPFTERS NGEINEKNVT PNPKQMLVTI V