HMP2_CAEEL
ID HMP2_CAEEL Reviewed; 678 AA.
AC O44326;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Beta-catenin-like protein hmp-2 {ECO:0000305};
DE AltName: Full=Protein humpback-2 {ECO:0000312|WormBase:K05C4.6a};
GN Name=hmp-2; ORFNames=K05C4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=9531567; DOI=10.1083/jcb.141.1.297;
RA Costa M., Raich W., Agbunag C., Leung B., Hardin J., Priess J.R.;
RT "A putative catenin-cadherin system mediates morphogenesis of the
RT Caenorhabditis elegans embryo.";
RL J. Cell Biol. 141:297-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH HMR-1.
RX PubMed=10952315; DOI=10.1038/35020099;
RA Korswagen H.C., Herman M.A., Clevers H.C.;
RT "Distinct beta-catenins mediate adhesion and signalling functions in C.
RT elegans.";
RL Nature 406:527-532(2000).
RN [4]
RP POSSIBLE INTERACTION WITH HMP-1.
RX PubMed=11560894; DOI=10.1093/genetics/159.1.159;
RA Natarajan L., Witwer N.E., Eisenmann D.M.;
RT "The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1
RT and HMP-2 make distinct protein interactions but retain functional
RT redundancy in vivo.";
RL Genetics 159:159-172(2001).
RN [5]
RP INTERACTION WITH FRK-1.
RX PubMed=20805471; DOI=10.1073/pnas.1006600107;
RA Putzke A.P., Rothman J.H.;
RT "Repression of Wnt signaling by a Fer-type nonreceptor tyrosine kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16154-16159(2010).
RN [6]
RP FUNCTION, INTERACTION WITH HMR-1, AND DISRUPTION PHENOTYPE.
RX PubMed=26412237; DOI=10.1016/j.devcel.2015.08.019;
RA Tsur A., Bening Abu-Shach U., Broday L.;
RT "ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens
RT Junctions.";
RL Dev. Cell 35:63-77(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 54-678 IN COMPLEX WITH HMR-1,
RP IDENTIFICATION IN CATENIN-CADHERIN COMPLEX, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-271 AND TYR-599.
RX PubMed=25850673; DOI=10.1016/j.devcel.2015.02.005;
RA Choi H.J., Loveless T., Lynch A.M., Bang I., Hardin J., Weis W.I.;
RT "A conserved phosphorylation switch controls the interaction between
RT cadherin and beta-catenin in vitro and in vivo.";
RL Dev. Cell 33:82-93(2015).
CC -!- FUNCTION: Required for cell migration during body enclosure and cell
CC shape changes during body elongation (PubMed:9531567). Plays a role in
CC recruitment of the cadherin protein hmr-1 to adherens junctions
CC (PubMed:26412237). {ECO:0000269|PubMed:26412237,
CC ECO:0000269|PubMed:9531567}.
CC -!- SUBUNIT: Component of a core catenin-cadherin complex consisting of
CC hmr-1, hmp-1 and hmp-2; the complex localizes to adherens junctions
CC (PubMed:25850673). Interacts with hmr-1; the interaction is direct
CC (PubMed:10952315, PubMed:25850673, PubMed:26412237). May interact with
CC hmp-1 (PubMed:11560894). Interacts with frk-1 (PubMed:20805471).
CC {ECO:0000269|PubMed:10952315, ECO:0000269|PubMed:11560894,
CC ECO:0000269|PubMed:20805471, ECO:0000269|PubMed:25850673,
CC ECO:0000269|PubMed:26412237}.
CC -!- INTERACTION:
CC O44326; Q967F4: hmr-1; NbExp=5; IntAct=EBI-317320, EBI-2528888;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:9531567}.
CC -!- TISSUE SPECIFICITY: Epidermal cells. {ECO:0000269|PubMed:9531567}.
CC -!- DEVELOPMENTAL STAGE: Present in all embryonic blastomeres at early
CC stages of development (at protein level). {ECO:0000269|PubMed:9531567}.
CC -!- DISRUPTION PHENOTYPE: Worms have strong elongation defects
CC (PubMed:9531567). RNAi-mediated knockdown results in failure of
CC cadherin protein hmr-1 to localize to adherens junctions, but results
CC in its accumulation along the basolateral membrane of the cell
CC (PubMed:26412237). {ECO:0000269|PubMed:26412237,
CC ECO:0000269|PubMed:9531567}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AF016853; AAB94552.1; -; mRNA.
DR EMBL; Z81564; CAB04572.1; -; Genomic_DNA.
DR PIR; T23341; T23341.
DR RefSeq; NP_001252426.1; NM_001265497.1.
DR PDB; 4R0Z; X-ray; 2.00 A; A=53-678.
DR PDB; 4R10; X-ray; 2.30 A; A=53-621.
DR PDB; 4R11; X-ray; 2.79 A; A/C/E=53-621.
DR PDB; 5XA5; X-ray; 1.60 A; B=36-79.
DR PDBsum; 4R0Z; -.
DR PDBsum; 4R10; -.
DR PDBsum; 4R11; -.
DR PDBsum; 5XA5; -.
DR AlphaFoldDB; O44326; -.
DR SMR; O44326; -.
DR BioGRID; 38723; 33.
DR ComplexPortal; CPX-499; Catenin-Cadherin complex.
DR DIP; DIP-27261N; -.
DR IntAct; O44326; 5.
DR STRING; 6239.K05C4.6b; -.
DR iPTMnet; O44326; -.
DR EPD; O44326; -.
DR PaxDb; O44326; -.
DR EnsemblMetazoa; K05C4.6a.1; K05C4.6a.1; WBGene00001979.
DR GeneID; 173338; -.
DR UCSC; K05C4.6; c. elegans.
DR CTD; 173338; -.
DR WormBase; K05C4.6a; CE19974; WBGene00001979; hmp-2.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000171121; -.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; O44326; -.
DR PhylomeDB; O44326; -.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-CEL-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-CEL-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-525793; Myogenesis.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR Reactome; R-CEL-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-CEL-8951430; RUNX3 regulates WNT signaling.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013106; RHOC GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR SignaLink; O44326; -.
DR PRO; PR:O44326; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001979; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O44326; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0016342; C:catenin complex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:WormBase.
DR GO; GO:0045296; F:cadherin binding; IPI:WormBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IGI:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; EXP:ComplexPortal.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IGI:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 1.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Developmental protein;
KW Reference proteome; Repeat.
FT CHAIN 1..678
FT /note="Beta-catenin-like protein hmp-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000268647"
FT REPEAT 153..192
FT /note="ARM 1"
FT REPEAT 280..319
FT /note="ARM 2"
FT REPEAT 320..359
FT /note="ARM 3"
FT REPEAT 362..403
FT /note="ARM 4"
FT REPEAT 409..448
FT /note="ARM 5"
FT MUTAGEN 271
FT /note="R->C: In zu364; embryonic lethal with embryos
FT failing to elongate and displaying a humpback phenotype in
FT which embryos contain a dorsal hump. Localizes exclusively
FT to the cytoplasm rather than adherens junctions."
FT /evidence="ECO:0000269|PubMed:25850673"
FT MUTAGEN 599
FT /note="Y->E: Phosphomimetic mutation. Initially localizes
FT to adherens junctions, but the distribution at the
FT junctions becomes punctate during late embryonic elongation
FT with excursions forming orthogonal to the junctions between
FT lateral seam cells and the dorsal and ventral neighboring
FT cells. Defects in F-actin filament organization that
FT include wavy and irregularly spaced filaments and the
FT occasional aggregation of multiple bundles at single points
FT along the adherens junction."
FT /evidence="ECO:0000269|PubMed:25850673"
FT MUTAGEN 599
FT /note="Y->F: Phospho-null mutation. No obvious phenotype."
FT /evidence="ECO:0000269|PubMed:25850673"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:4R0Z"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 388..401
FT /evidence="ECO:0007829|PDB:4R0Z"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 433..446
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 467..484
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 495..509
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 554..566
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:4R0Z"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:4R0Z"
FT HELIX 594..611
FT /evidence="ECO:0007829|PDB:4R0Z"
SQ SEQUENCE 678 AA; 74511 MW; E6C7ED51F6241232 CRC64;
MLLHSTNSYS IFTDHEVETR TSRIRSAMFP DWIPPTSAAE ATNSTTSIVE MMQMPTQQLK
QSVMDLLTYE GSNDMSGLSL PDLVKLMCDH DESVVARAVH RAYMLSREDP NFFNAPGFDH
RSFVEALMAA SKSSNVNVRR NAIGALSHMS EQRGGPLLIF RSGGLAEIIR MLYDSLESVV
HYAVTTLRNL LMHVSDSRAQ ARALNAVEAL TPHLHKTNPK LLAQVADGLY FLLIDDAPSK
ITFLSLLGPQ ILVSILREYS DHRKLIYTVV RCIRSLSVCP SNKPALISLG CLPALYVELC
TAKDERSQTA ILVAMRNLSD SATNEENLTQ LIIKLLEIIR VANDGMTACA CGTLSNLTCN
NTRNKQTVCS HGGIDALVTA IRRLPEVEEV TEPALCALRH CTARHSLAEE AQSELRFCQA
FPVILDQLET LRTPVIKAAL GVIRNSALLQ TNLIELTQEQ TANGHTAVSL TMDILRRAIT
AIEENPDIAV DGVPMWGVIE GAVSALHQLA NHPAVAAACC DDIGQVGNPE CPPFLDLLHR
LLAHPRLGSM DDEVLEREIL GLLYQLSKRP DGARAVESTG VSALLMESRG SQYKSVVTYA
NGVLSNLKRG DSAAIMNMSN SYDYEMSGSA ADWQRDGLER ELFAEMYPTN DGGHSESINM
ALNNSQMRPN HNWYDTDL
