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Beta-catenin-like protein hmp-2 (Protein humpback-2)

 HMP2_CAEEL              Reviewed;         678 AA.
O44326;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=Beta-catenin-like protein hmp-2 {ECO:0000305};
AltName: Full=Protein humpback-2 {ECO:0000312|WormBase:K05C4.6a};
Name=hmp-2; ORFNames=K05C4.6;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=Bristol N2;
PubMed=9531567; DOI=10.1083/jcb.141.1.297;
Costa M., Raich W., Agbunag C., Leung B., Hardin J., Priess J.R.;
"A putative catenin-cadherin system mediates morphogenesis of the
Caenorhabditis elegans embryo.";
J. Cell Biol. 141:297-308(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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]
INTERACTION WITH HMR-1.
PubMed=10952315; DOI=10.1038/35020099;
Korswagen H.C., Herman M.A., Clevers H.C.;
"Distinct beta-catenins mediate adhesion and signalling functions in
C. elegans.";
Nature 406:527-532(2000).
[4]
POSSIBLE INTERACTION WITH HMP-1.
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]
INTERACTION WITH FRK-1.
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).
[6]
FUNCTION, INTERACTION WITH HMR-1, AND DISRUPTION PHENOTYPE.
PubMed=26412237; DOI=10.1016/j.devcel.2015.08.019;
Tsur A., Bening Abu-Shach U., Broday L.;
"ULP-2 SUMO Protease Regulates E-Cadherin Recruitment to Adherens
Junctions.";
Dev. Cell 35:63-77(2015).
[7]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 54-678 IN COMPLEX WITH
HMR-1, IDENTIFICATION IN CATENIN-CADHERIN COMPLEX, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF ARG-271 AND TYR-599.
PubMed=25850673; DOI=10.1016/j.devcel.2015.02.005;
Choi H.J., Loveless T., Lynch A.M., Bang I., Hardin J., Weis W.I.;
"A conserved phosphorylation switch controls the interaction between
cadherin and beta-catenin in vitro and in vivo.";
Dev. Cell 33:82-93(2015).
-!- FUNCTION: Required for cell migration during body enclosure and
cell shape changes during body elongation (PubMed:9531567). Plays
a role in recruitment of the cadherin protein hmr-1 to adherens
junctions (PubMed:26412237). {ECO:0000269|PubMed:26412237,
ECO:0000269|PubMed:9531567}.
-!- SUBUNIT: Component of a core catenin-cadherin complex consisting
of hmr-1, hmp-1 and hmp-2; the complex localizes to adherens
junctions (PubMed:25850673). Interacts with hmr-1; the interaction
is direct (PubMed:10952315, PubMed:25850673, PubMed:26412237). May
interact with hmp-1 (PubMed:11560894). Interacts with frk-1
(PubMed:20805471). {ECO:0000269|PubMed:10952315,
ECO:0000269|PubMed:11560894, ECO:0000269|PubMed:20805471,
ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:26412237}.
-!- INTERACTION:
Q967F4:hmr-1; NbExp=5; IntAct=EBI-317320, EBI-2528888;
-!- SUBCELLULAR LOCATION: Cell junction, adherens junction
{ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:9531567}.
-!- TISSUE SPECIFICITY: Epidermal cells. {ECO:0000269|PubMed:9531567}.
-!- DEVELOPMENTAL STAGE: Present in all embryonic blastomeres at early
stages of development (at protein level).
{ECO:0000269|PubMed:9531567}.
-!- DISRUPTION PHENOTYPE: Worms have strong elongation defects
(PubMed:9531567). RNAi-mediated knockdown results in failure of
cadherin protein hmr-1 to localize to adherens junctions, but
results in its accumulation along the basolateral membrane of the
cell (PubMed:26412237). {ECO:0000269|PubMed:26412237,
ECO:0000269|PubMed:9531567}.
-!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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EMBL; AF016853; AAB94552.1; -; mRNA.
EMBL; Z81564; CAB04572.1; -; Genomic_DNA.
PIR; T23341; T23341.
RefSeq; NP_001252426.1; NM_001265497.1.
UniGene; Cel.7074; -.
PDB; 4R0Z; X-ray; 2.00 A; A=53-678.
PDB; 4R10; X-ray; 2.30 A; A=53-621.
PDB; 4R11; X-ray; 2.79 A; A/C/E=53-621.
PDB; 5XA5; X-ray; 1.60 A; B=36-79.
PDBsum; 4R0Z; -.
PDBsum; 4R10; -.
PDBsum; 4R11; -.
PDBsum; 5XA5; -.
ProteinModelPortal; O44326; -.
SMR; O44326; -.
BioGrid; 38723; 20.
ComplexPortal; CPX-499; Catenin-Cadherin complex.
DIP; DIP-27261N; -.
IntAct; O44326; 5.
STRING; 6239.K05C4.6b; -.
EPD; O44326; -.
PaxDb; O44326; -.
EnsemblMetazoa; K05C4.6a.1; K05C4.6a.1; WBGene00001979.
EnsemblMetazoa; K05C4.6a.2; K05C4.6a.2; WBGene00001979.
GeneID; 173338; -.
UCSC; K05C4.6; c. elegans.
CTD; 173338; -.
WormBase; K05C4.6a; CE19974; WBGene00001979; hmp-2.
eggNOG; KOG4203; Eukaryota.
eggNOG; COG0035; LUCA.
GeneTree; ENSGT00730000110821; -.
HOGENOM; HOG000021706; -.
InParanoid; O44326; -.
PhylomeDB; O44326; -.
Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-CEL-6798695; Neutrophil degranulation.
SignaLink; O44326; -.
PRO; PR:O44326; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00001979; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
ExpressionAtlas; O44326; baseline and differential.
GO; GO:0016342; C:catenin complex; IDA:WormBase.
GO; GO:0005913; C:cell-cell adherens junction; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0045294; F:alpha-catenin binding; IPI:WormBase.
GO; GO:0045296; F:cadherin binding; IPI:WormBase.
GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
GO; GO:0016477; P:cell migration; IMP:WormBase.
GO; GO:0042074; P:cell migration involved in gastrulation; IGI:WormBase.
GO; GO:0002159; P:desmosome assembly; IEA:InterPro.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:UniProtKB.
GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; IGI:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; IMP:WormBase.
GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
GO; GO:0044333; P:Wnt signaling pathway involved in digestive tract morphogenesis; IGI:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR013284; Beta-catenin.
InterPro; IPR030461; Plakoglobin/HMP-2.
PANTHER; PTHR23315:SF12; PTHR23315:SF12; 1.
Pfam; PF00514; Arm; 1.
PRINTS; PR01869; BCATNINFAMLY.
SMART; SM00185; ARM; 8.
SUPFAM; SSF48371; SSF48371; 2.
PROSITE; PS50176; ARM_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell junction; Complete proteome;
Developmental protein; Reference proteome; Repeat.
CHAIN 1 678 Beta-catenin-like protein hmp-2.
{ECO:0000305}.
/FTId=PRO_0000268647.
REPEAT 153 192 ARM 1.
REPEAT 280 319 ARM 2.
REPEAT 320 359 ARM 3.
REPEAT 362 403 ARM 4.
REPEAT 409 448 ARM 5.
MUTAGEN 271 271 R->C: In zu364; embryonic lethal with
embryos failing to elongate and
displaying a humpback phenotype in which
embryos contain a dorsal hump. Localizes
exclusively to the cytoplasm rather than
adherens junctions.
{ECO:0000269|PubMed:25850673}.
MUTAGEN 599 599 Y->E: Phosphomimetic mutation. Initially
localizes to adherens junctions, but the
distribution at the junctions becomes
punctate during late embryonic elongation
with excursions forming orthogonal to the
junctions between lateral seam cells and
the dorsal and ventral neighboring cells.
Defects in F-actin filament organization
that include wavy and irregularly spaced
filaments and the occasional aggregation
of multiple bundles at single points
along the adherens junction.
{ECO:0000269|PubMed:25850673}.
MUTAGEN 599 599 Y->F: Phospho-null mutation. No obvious
phenotype. {ECO:0000269|PubMed:25850673}.
HELIX 48 51 {ECO:0000244|PDB:5XA5}.
HELIX 53 67 {ECO:0000244|PDB:5XA5}.
HELIX 80 89 {ECO:0000244|PDB:4R0Z}.
HELIX 92 108 {ECO:0000244|PDB:4R0Z}.
HELIX 110 114 {ECO:0000244|PDB:4R0Z}.
HELIX 120 130 {ECO:0000244|PDB:4R0Z}.
HELIX 136 149 {ECO:0000244|PDB:4R0Z}.
HELIX 155 162 {ECO:0000244|PDB:4R0Z}.
HELIX 165 170 {ECO:0000244|PDB:4R0Z}.
HELIX 171 173 {ECO:0000244|PDB:4R0Z}.
HELIX 177 193 {ECO:0000244|PDB:4R0Z}.
HELIX 197 203 {ECO:0000244|PDB:4R0Z}.
HELIX 206 210 {ECO:0000244|PDB:4R0Z}.
HELIX 211 215 {ECO:0000244|PDB:4R0Z}.
HELIX 219 233 {ECO:0000244|PDB:4R0Z}.
HELIX 237 245 {ECO:0000244|PDB:4R0Z}.
HELIX 248 258 {ECO:0000244|PDB:4R0Z}.
HELIX 263 276 {ECO:0000244|PDB:4R0Z}.
HELIX 282 288 {ECO:0000244|PDB:4R0Z}.
HELIX 291 301 {ECO:0000244|PDB:4R0Z}.
HELIX 305 318 {ECO:0000244|PDB:4R0Z}.
HELIX 319 321 {ECO:0000244|PDB:4R0Z}.
HELIX 329 338 {ECO:0000244|PDB:4R0Z}.
TURN 339 341 {ECO:0000244|PDB:4R0Z}.
HELIX 344 358 {ECO:0000244|PDB:4R0Z}.
HELIX 362 370 {ECO:0000244|PDB:4R0Z}.
HELIX 373 383 {ECO:0000244|PDB:4R0Z}.
HELIX 388 401 {ECO:0000244|PDB:4R0Z}.
STRAND 403 405 {ECO:0000244|PDB:4R0Z}.
HELIX 408 417 {ECO:0000244|PDB:4R0Z}.
HELIX 421 428 {ECO:0000244|PDB:4R0Z}.
HELIX 433 446 {ECO:0000244|PDB:4R0Z}.
HELIX 452 458 {ECO:0000244|PDB:4R0Z}.
HELIX 467 484 {ECO:0000244|PDB:4R0Z}.
HELIX 495 509 {ECO:0000244|PDB:4R0Z}.
HELIX 513 521 {ECO:0000244|PDB:4R0Z}.
HELIX 534 542 {ECO:0000244|PDB:4R0Z}.
HELIX 545 548 {ECO:0000244|PDB:4R0Z}.
HELIX 554 566 {ECO:0000244|PDB:4R0Z}.
HELIX 570 577 {ECO:0000244|PDB:4R0Z}.
TURN 578 580 {ECO:0000244|PDB:4R0Z}.
HELIX 582 588 {ECO:0000244|PDB:4R0Z}.
HELIX 594 611 {ECO:0000244|PDB:4R0Z}.
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


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