HMP1_CAEEL
ID HMP1_CAEEL Reviewed; 927 AA.
AC P90947;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-catenin-like protein hmp-1 {ECO:0000305};
DE AltName: Full=Protein humpback-1 {ECO:0000312|WormBase:R13H4.4a};
GN Name=hmp-1; ORFNames=R13H4.4;
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 POSSIBLE INTERACTION WITH HMP-2.
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 [4]
RP FUNCTION, IDENTIFICATION IN CATENIN-CADHERIN COMPLEX, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=25938815; DOI=10.1038/ncb3168;
RA Klompstra D., Anderson D.C., Yeh J.Y., Zilberman Y., Nance J.;
RT "An instructive role for C. elegans E-cadherin in translating cell contact
RT cues into cortical polarity.";
RL Nat. Cell Biol. 17:726-735(2015).
CC -!- FUNCTION: Required for cell migration during body enclosure and cell
CC shape changes during body elongation (PubMed:9531567). Required for
CC proper localization of other junctional components, such as pac-1
CC (PubMed:25938815). {ECO:0000269|PubMed:25938815,
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 (Probable). May interact with hmp-2 (PubMed:11560894).
CC {ECO:0000269|PubMed:11560894, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}. Cytoplasm
CC {ECO:0000269|PubMed:25938815}.
CC -!- TISSUE SPECIFICITY: Epidermal cells. {ECO:0000269|PubMed:9531567}.
CC -!- DEVELOPMENTAL STAGE: Present in all embryonic blastomeres at early
CC stages of development. {ECO:0000269|PubMed:25938815,
CC ECO:0000269|PubMed:9531567}.
CC -!- DISRUPTION PHENOTYPE: Worms arrest their elongation at the 1.25X to
CC 1.5X stage. {ECO:0000269|PubMed:9531567}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AF016852; AAB94551.1; -; mRNA.
DR EMBL; Z81579; CAB61019.1; -; Genomic_DNA.
DR RefSeq; NP_505985.1; NM_073584.4.
DR PDB; 5H5M; X-ray; 2.40 A; A/B=267-646.
DR PDB; 5XA5; X-ray; 1.60 A; A=2-275.
DR PDBsum; 5H5M; -.
DR PDBsum; 5XA5; -.
DR AlphaFoldDB; P90947; -.
DR SMR; P90947; -.
DR BioGRID; 44648; 25.
DR ComplexPortal; CPX-499; Catenin-Cadherin complex.
DR DIP; DIP-61638N; -.
DR IntAct; P90947; 1.
DR STRING; 6239.R13H4.4b; -.
DR iPTMnet; P90947; -.
DR EPD; P90947; -.
DR PaxDb; P90947; -.
DR PRIDE; P90947; -.
DR EnsemblMetazoa; R13H4.4a.1; R13H4.4a.1; WBGene00001978.
DR GeneID; 179624; -.
DR UCSC; R13H4.4a; c. elegans.
DR CTD; 179624; -.
DR WormBase; R13H4.4a; CE25089; WBGene00001978; hmp-1.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; P90947; -.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-525793; Myogenesis.
DR SignaLink; P90947; -.
DR PRO; PR:P90947; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001978; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P90947; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0043296; C:apical junction complex; IDA:WormBase.
DR GO; GO:0016342; C:catenin complex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0008013; F:beta-catenin binding; IPI:WormBase.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
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:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR006077; Vinculin/catenin.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW Developmental protein; Reference proteome.
FT CHAIN 1..927
FT /note="Alpha-catenin-like protein hmp-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000268648"
FT REGION 901..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..354
FT /evidence="ECO:0000255"
FT COILED 672..696
FT /evidence="ECO:0000255"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 47..70
FT /evidence="ECO:0007829|PDB:5XA5"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 79..108
FT /evidence="ECO:0007829|PDB:5XA5"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 113..161
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 165..192
FT /evidence="ECO:0007829|PDB:5XA5"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 196..225
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 230..254
FT /evidence="ECO:0007829|PDB:5XA5"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:5H5M"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 292..314
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 321..345
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 357..387
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:5H5M"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 407..431
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 438..467
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 472..498
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 502..525
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 541..565
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 570..584
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 586..604
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:5H5M"
FT HELIX 610..639
FT /evidence="ECO:0007829|PDB:5H5M"
SQ SEQUENCE 927 AA; 103994 MW; 8F3DCB97613B88AA CRC64;
MPANGNSHAY FNIDEVRSKN VLKQITQLIN EVTNITETFP LKPGQTTEGL VATLDAAVAN
FLQTGSFAIS KCPIANSDPR AIDLLHEALG AVQDTGQVMI QTGRDFVRDS TSTNKRAIAT
NSGRNLLTAV AKFLILADSI DVKVIVDKVD EVRETAHQMI EADTKIKVDD LYNLLISQIE
ELDITVRRRA IDLVKPNQRD DLLAARSALR QTAPLLYTST RTFVRHPEHE EARRNRDYTA
DEMHSALNAL ESVLNGQQPK VTFSEYGRIG DLINEIDTFQ NRIEIDPAHY RRGTDRPDLE
GHCERIVSGS ASIADAESTR ENRKQKIVAE CNNLRQALQE LLTEYEKSTG RRDDNDDIPL
GIAEVHKRTK DLRRHLRRAI VDHISDAFLD TRTPLILLIE AAKEGHEENT RYRSKMFQEH
ANEIVSVARL SCQLSSDVES VSVIQHTAAQ LEKLAPQVAQ AAILLCHQPT SKTAQENMET
YKNAWFDKVR LLTTALDNIT TLDDFLAVSE AHIVEDCERG IKGITANAST PDENAANCET
VDCAAGSIRG RALRVCDVVD AEMDFLQNSE YTETVKQAVR ILKTQRVDQF AERASALANR
QEAHGLTWDP KTKEEEMNEF INACTLVHDA VKDIRHALLM NRSMNDVDSD VEYEADGVGA
ANADANRTIS EQENQQNLMR RLPEEEKKKI QAQIDIFKVT QTRFEREVAK WDETGNDIIS
LANNMCKIMM SMTEFTRGCG PLKTTMDVIR AAQEISLNGS KLNALARQIG EESADSQTKK
DLLAYLSQIT LYCQQLNICS KVKADVTQVG NELVVSALDS AMSLIQTARN LLTAVVQTVK
AAYIASTKFR RPNANSVRVE WRMAPPKKQP LIRPQKNNAI IRRASERRPL QPAKVLAEFT
RNEIETGRDS DDEELDRRHQ QRINGRL
