HMR1_CAEEL
ID HMR1_CAEEL Reviewed; 2920 AA.
AC Q967F4; B2MZC5; H2FLJ9; H2FLK0; O44327;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cadherin-related hmr-1;
DE AltName: Full=Protein Hammerhead;
DE Flags: Precursor;
GN Name=hmr-1; ORFNames=W02B9.1;
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] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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 [MRNA] (ISOFORM B), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=11790304; DOI=10.1016/s0960-9822(01)00624-8;
RA Broadbent I.D., Pettitt J.;
RT "The C. elegans hmr-1 gene can encode a neuronal classic cadherin involved
RT in the regulation of axon fasciculation.";
RL Curr. Biol. 12:59-63(2002).
RN [3]
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 [4]
RP INTERACTION WITH HMP-2.
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 [5]
RP FUNCTION, INTERACTION WITH JAC-1, AND SUBCELLULAR LOCATION.
RX PubMed=12847081; DOI=10.1083/jcb.200212136;
RA Pettitt J., Cox E.A., Broadbent I.D., Flett A., Hardin J.;
RT "The Caenorhabditis elegans p120 catenin homologue, JAC-1, modulates
RT cadherin-catenin function during epidermal morphogenesis.";
RL J. Cell Biol. 162:15-22(2003).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2623, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2623, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20515680; DOI=10.1016/j.ydbio.2010.05.507;
RA Grana T.M., Cox E.A., Lynch A.M., Hardin J.;
RT "SAX-7/L1CAM and HMR-1/cadherin function redundantly in blastomere
RT compaction and non-muscle myosin accumulation during Caenorhabditis elegans
RT gastrulation.";
RL Dev. Biol. 344:731-744(2010).
RN [9]
RP SUBUNIT, INTERACTION WITH HMP-2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20689042; DOI=10.1073/pnas.1007349107;
RA Kwiatkowski A.V., Maiden S.L., Pokutta S., Choi H.J., Benjamin J.M.,
RA Lynch A.M., Nelson W.J., Weis W.I., Hardin J.;
RT "In vitro and in vivo reconstitution of the cadherin-catenin-actin complex
RT from Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14591-14596(2010).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22675206; DOI=10.1242/dev.079863;
RA Chihara D., Nance J.;
RT "An E-cadherin-mediated hitchhiking mechanism for C. elegans germ cell
RT internalization during gastrulation.";
RL Development 139:2547-2556(2012).
RN [11]
RP FUNCTION, INTERACTION WITH JAC-1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
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).
RN [12]
RP INTERACTION WITH HMP-2, SUBCELLULAR LOCATION, SUMOYLATION, AND MUTAGENESIS
RP OF LYS-2845; LYS-2874; LYS-2882 AND LYS-2884.
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2841-2920 IN COMPLEX WITH HMP-2,
RP FUNCTION, IDENTIFICATION IN CATENIN-CADHERIN COMPLEX, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-2839; SER-2909; THR-2912;
RP SER-2915 AND SER-2918, AND MUTAGENESIS OF SER-2909 AND THR-2912.
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: Cadherins are calcium-dependent cell adhesion proteins
CC (PubMed:25938815, PubMed:25850673). They preferentially interact with
CC themselves in a homophilic manner in connecting cells; cadherins may
CC thus contribute to the sorting of heterogeneous cell types
CC (PubMed:25938815, PubMed:25850673). Required for adherens junction
CC assembly and connecting adherens junctions to the cytoskeleton
CC (PubMed:26412237). {ECO:0000269|PubMed:25850673,
CC ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:26412237}.
CC -!- FUNCTION: Isoform a is required for cell migration during body
CC enclosure and cell shape changes during body elongation
CC (PubMed:9531567, PubMed:12847081). Required for proper localization of
CC other junctional components, such as hmp-1, hmp-2, jac-1 and pac-1
CC (PubMed:9531567, PubMed:25938815). Recruitment of pac-1 is required to
CC establish cell polarity, independent of its role in cell adhesion
CC (PubMed:25938815). Required for primodial germ cell ingression and
CC adherence to endodermal cells during gastrulation (PubMed:20515680,
CC PubMed:22675206). {ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:20515680, ECO:0000269|PubMed:22675206,
CC ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}.
CC -!- FUNCTION: Isoform b is involved in axonal guidance in a subset of motor
CC neurons. {ECO:0000269|PubMed:11790304}.
CC -!- SUBUNIT: Monomer in solution (PubMed:20689042). Isoform a is a
CC component of a core catenin-cadherin complex consisting of hmr-1, hmp-1
CC and hmp-2; the complex localizes to adherens junctions
CC (PubMed:20689042, PubMed:25850673). Isoform a interacts with hmp-2; the
CC interaction is direct (PubMed:10952315, PubMed:20689042,
CC PubMed:25850673, PubMed:26412237). Isoform a interacts (via
CC intracellular domain) with jac-1 (PubMed:12847081, PubMed:25938815).
CC {ECO:0000269|PubMed:10952315, ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:20689042, ECO:0000269|PubMed:25850673,
CC ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:26412237}.
CC -!- INTERACTION:
CC Q967F4; O44326: hmp-2; NbExp=5; IntAct=EBI-2528888, EBI-317320;
CC Q967F4; Q9U308: jac-1; NbExp=3; IntAct=EBI-2528888, EBI-2917356;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:9531567}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:20515680,
CC ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:25938815,
CC ECO:0000269|PubMed:26412237}. Cell junction
CC {ECO:0000269|PubMed:20689042}. Note=The basal to apical translocation
CC from the cell membrane to adherens junctions is determined by the
CC coupled sumoylation and desumoylation state of hmr-1.
CC {ECO:0000269|PubMed:26412237}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cell junction, adherens junction
CC {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:25850673}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=b;
CC IsoId=Q967F4-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q967F4-2; Sequence=VSP_021978, VSP_021979;
CC Name=c;
CC IsoId=Q967F4-3; Sequence=VSP_044150, VSP_044153;
CC Name=d;
CC IsoId=Q967F4-4; Sequence=VSP_044151;
CC Name=e;
CC IsoId=Q967F4-5; Sequence=VSP_044152;
CC -!- TISSUE SPECIFICITY: Isoform b is neuron-specific (PubMed:11790304).
CC Isoform a is located in epidermal cells (at protein level)
CC (PubMed:9531567). {ECO:0000269|PubMed:11790304,
CC ECO:0000269|PubMed:9531567}.
CC -!- DEVELOPMENTAL STAGE: Isoform a is present in all embryonic blastomeres
CC at early stages of development (PubMed:9531567, PubMed:25938815).
CC Expressed throughout gastrulation and in primordial germ cells
CC (PubMed:22675206). {ECO:0000269|PubMed:22675206,
CC ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}.
CC -!- DOMAIN: The cytoplasmic domain is necessary for binding to jac-1.
CC {ECO:0000269|PubMed:25938815}.
CC -!- PTM: Phosphorylation at T-2912 increases the binding affinity for hmp-
CC 2. {ECO:0000269|PubMed:25850673}.
CC -!- PTM: Sumoylated. Sumoylation prevents accumulation at adherens
CC junctions and decreases the binding affinity for hmp-2.
CC {ECO:0000269|PubMed:26412237}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:20689042,
CC PubMed:25850673). Hammerhead phenotype characterized by morphogenetic
CC defects before the start of body elongation, due to improper closure of
CC hypodermis (PubMed:9531567, PubMed:25850673). Humpback phenotype with
CC embryos containing dorsal humps (PubMed:20689042). Embryos also exhibit
CC defective actin structures including loss of actin at cell-cell
CC junctions and detached thick actin bundles called circumferential
CC filament bundles that insert at right angles to junctional actin
CC (PubMed:20689042). RNAi-mediated knockdown results in ingression
CC defects in primordial germ cells (PubMed:22675206).
CC {ECO:0000269|PubMed:20689042, ECO:0000269|PubMed:22675206,
CC ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:9531567}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB94553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF016854; AAB94553.1; ALT_INIT; mRNA.
DR EMBL; AJ307058; CAC38842.1; -; mRNA.
DR EMBL; Z82064; CAB61036.2; -; Genomic_DNA.
DR EMBL; Z82064; CAD27611.1; -; Genomic_DNA.
DR EMBL; AL032638; CAD27611.1; JOINED; Genomic_DNA.
DR EMBL; Z82093; CAD27611.1; JOINED; Genomic_DNA.
DR EMBL; Z82064; CAQ48404.1; -; Genomic_DNA.
DR EMBL; Z82064; CCF23411.1; -; Genomic_DNA.
DR EMBL; Z82064; CCF23412.1; -; Genomic_DNA.
DR RefSeq; NP_001021649.2; NM_001026478.3.
DR RefSeq; NP_001021650.1; NM_001026479.2. [Q967F4-1]
DR RefSeq; NP_001129794.1; NM_001136322.1.
DR RefSeq; NP_001251561.1; NM_001264632.1. [Q967F4-4]
DR RefSeq; NP_001251562.1; NM_001264633.1.
DR PDB; 4R10; X-ray; 2.30 A; B=2841-2920.
DR PDB; 4R11; X-ray; 2.79 A; B/D/F=2841-2920.
DR PDBsum; 4R10; -.
DR PDBsum; 4R11; -.
DR SMR; Q967F4; -.
DR BioGRID; 38416; 10.
DR ComplexPortal; CPX-499; Catenin-Cadherin complex.
DR DIP; DIP-56285N; -.
DR IntAct; Q967F4; 10.
DR STRING; 6239.W02B9.1b; -.
DR iPTMnet; Q967F4; -.
DR EPD; Q967F4; -.
DR PaxDb; Q967F4; -.
DR PeptideAtlas; Q967F4; -.
DR EnsemblMetazoa; W02B9.1a.1; W02B9.1a.1; WBGene00001980. [Q967F4-2]
DR EnsemblMetazoa; W02B9.1a.2; W02B9.1a.2; WBGene00001980. [Q967F4-2]
DR EnsemblMetazoa; W02B9.1b.1; W02B9.1b.1; WBGene00001980. [Q967F4-1]
DR EnsemblMetazoa; W02B9.1d.1; W02B9.1d.1; WBGene00001980. [Q967F4-4]
DR EnsemblMetazoa; W02B9.1e.1; W02B9.1e.1; WBGene00001980. [Q967F4-5]
DR GeneID; 173007; -.
DR KEGG; cel:CELE_W02B9.1; -.
DR UCSC; W02B9.1b; c. elegans. [Q967F4-1]
DR CTD; 173007; -.
DR WormBase; W02B9.1a; CE46853; WBGene00001980; hmr-1. [Q967F4-2]
DR WormBase; W02B9.1b; CE30357; WBGene00001980; hmr-1. [Q967F4-1]
DR WormBase; W02B9.1c; CE42574; WBGene00001980; hmr-1. [Q967F4-3]
DR WormBase; W02B9.1d; CE46949; WBGene00001980; hmr-1. [Q967F4-4]
DR WormBase; W02B9.1e; CE47071; WBGene00001980; hmr-1. [Q967F4-5]
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000168029; -.
DR HOGENOM; CLU_000347_1_0_1; -.
DR InParanoid; Q967F4; -.
DR OMA; YPQFYEV; -.
DR OrthoDB; 6237at2759; -.
DR PhylomeDB; Q967F4; -.
DR SignaLink; Q967F4; -.
DR PRO; PR:Q967F4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001980; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0016342; C:catenin complex; IDA:WormBase.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:WormBase.
DR GO; GO:0008013; F:beta-catenin binding; IPI:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070097; F:delta-catenin binding; IPI:WormBase.
DR GO; GO:0003384; P:apical constriction involved in gastrulation; IGI:WormBase.
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:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR GO; GO:0007369; P:gastrulation; IGI:WormBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 13.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 13.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 8.
DR PROSITE; PS50268; CADHERIN_2; 15.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2920
FT /note="Cadherin-related hmr-1"
FT /id="PRO_0000268646"
FT TOPO_DOM 20..2779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2780..2800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2801..2920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 322..422
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 425..530
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 531..642
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 643..747
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 749..865
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 871..979
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 980..1093
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1097..1211
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1212..1335
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1336..1436
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1438..1546
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1548..1661
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1662..1772
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1772..1874
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2246..2283
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2284..2478
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2492..2527
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 2858..2891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2870..2891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2839
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25850673"
FT MOD_RES 2909
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25850673"
FT MOD_RES 2912
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25850673"
FT MOD_RES 2915
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25850673"
FT MOD_RES 2918
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25850673"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633"
FT DISULFID 2250..2261
FT /evidence="ECO:0000250"
FT DISULFID 2255..2270
FT /evidence="ECO:0000250"
FT DISULFID 2272..2282
FT /evidence="ECO:0000250"
FT DISULFID 2452..2478
FT /evidence="ECO:0000250"
FT DISULFID 2501..2515
FT /evidence="ECO:0000250"
FT DISULFID 2517..2526
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1986
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_044152"
FT VAR_SEQ 1..1856
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_044151"
FT VAR_SEQ 1..1747
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044150"
FT VAR_SEQ 1..1651
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9531567"
FT /id="VSP_021978"
FT VAR_SEQ 1652..1805
FT /note="TDMNDNAPFFEKTRYEGSVEETAPIGAAVMSFSAFDADEEAKDNVFTYQLSE
FT ESDYFYVTTDKDSKQSSVGVLRVKQPLDYEDVTQRDGFHLGIRVSDGRHDAEAAVHVAL
FT VDRNDHAPHIHGATEHRVREDVPRGTSIGRYTATDRDAGDTAR -> MQKRRCTWHSSI
FT ATTTRHTFTEPQNTESERTCHVEQALDDTRQRIGMPETRQGRSSRGNCVIFGSSKRLWV
FT TLLGFCFVLSTLIGGAEAFTDLSLPFGLEPSVAKSRFSSLVGGVRARDIHVFVMKNISE
FT DTPVGTVLETFKAHDPSNPMYNFS (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9531567"
FT /id="VSP_021979"
FT VAR_SEQ 1748..1805
FT /note="SDGRHDAEAAVHVALVDRNDHAPHIHGATEHRVREDVPRGTSIGRYTATDRD
FT AGDTAR -> MANFWLFSLHPKLTRWVIRWICEGEASPLPLLILIYNGNNKCNGVKKKK
FT KKKKKKKKK (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044153"
FT MUTAGEN 2845
FT /note="K->R: No obvious phenotype."
FT /evidence="ECO:0000269|PubMed:26412237"
FT MUTAGEN 2874
FT /note="K->R: No obvious phenotype. No sumoylation; when
FT associated with R-2882 and R-2884."
FT /evidence="ECO:0000269|PubMed:26412237"
FT MUTAGEN 2882
FT /note="K->R: No sumoylation; when associated with R-2874
FT and R-2884."
FT /evidence="ECO:0000269|PubMed:26412237"
FT MUTAGEN 2884
FT /note="K->R: No sumoylation; when associated with R-2874
FT and R-2882."
FT /evidence="ECO:0000269|PubMed:26412237"
FT MUTAGEN 2909
FT /note="S->A: Results in no phosphorylation at S-2909, T-
FT 2912, S-2915 and S-2918. Retains ability to bind to hmp-2."
FT /evidence="ECO:0000269|PubMed:25850673"
FT MUTAGEN 2912
FT /note="T->A: Results in no phosphorylation at S-2915 and S-
FT 2918. Upon phosphorylation by kin-19, there is increased
FT binding to hmp-2."
FT /evidence="ECO:0000269|PubMed:25850673"
FT STRAND 2844..2847
FT /evidence="ECO:0007829|PDB:4R10"
FT HELIX 2877..2888
FT /evidence="ECO:0007829|PDB:4R10"
FT HELIX 2890..2892
FT /evidence="ECO:0007829|PDB:4R10"
FT STRAND 2896..2899
FT /evidence="ECO:0007829|PDB:4R10"
SQ SEQUENCE 2920 AA; 323914 MW; 5E0D4C8FD24694FB CRC64;
MSWNILLILL ISNLDEVLAK TLLKLPSNAP PGWLISDLQF QNLIGDSEIA TLQPSIFSTN
FEVEDGYRII TNTTVTQFHG ELFELFLNVK EQNFQRLVTL HVYVDPRGTS QQPATFLSTV
YHATVYTSQQ PGSTVVFSKP ITVRNRKNFV ISPISKIDKI SKYSSPFSVM TRGKSVDIVM
MKQKLEEDDI TRHVIFLGAF TEKTGEMIAQ TKVIIDVIDS GDVHFLLKSK KSIAKFASAI
PANSTVFDVE KRNLSEPLLF HLEEPSRFFK IDQFSGRVST VLPVGYGTYH IHVVARNQKK
QRSDAWLEIS VKKEQKLEPM TSSRSRRHLD DIVFRIPENT TMEDIEKKDM KIPLFAGETI
GEINVAKEWL KIDDDGKIHL LKPLNYEKTS SIIATVPING LQSTRTQTIR IHVADIDEPP
SFVNSPLPML AVVPLNPTIG RIVYQFVARD EHGDGDSNVL YKTIDVIPAG SFIVDPKSGV
VRTGWSKYER GDTYRISAQA MDLSPSDNTT SQLSEVAILE ILADERPPQF AKQEYEVTVS
EDNLVDYSVV DVKAQSFRSF EDGRSKGPIT YSLEGDTPED ETKWFRIDPS TGIIHLTRLL
DFDDPALPKL HKLKVTARED NRESHVDLTI RIDDVNDNVP TFTRPLYTAQ VREDIPLNQT
ILKVTAVDKD TGDNSRITYS VDNHNFSINS NGEISAKVRL DADQLNERHF VYRFNVTARD
HGEPVSLSSS AMIHIRTENT NDESAVFLPT SQYTAFVAED AQGGTPVIQI QARDADRDEV
TYSFMDKNGR STQKMNLFSI DEHTGLVKLR HGVSAADLAE AENPINLTVI VQDDGSCCVY
PSKTHTSYAT LLIGIEDVNN NKPEFPDCAK YSDIAKIMEG TYKTDPPTIV KVEATDDDSS
ANGDIVYSLY YTQSESRKAF VIDRQTGVLT PSPHVVFDRE TRPREDVTVK ATDRGDRPLI
GFCQFSVEVV DINDNSPQFE RPSYETSVSR FEAVGTSVIT VFAFDNDAAH NAEITYSLEI
DTTAGEEHQN DLDFFELVNR RSGEITLIKP IPMKTQKFIF NVIADDNGIP EALQSSAQVT
LNVLDKQQKA PKWQTSPDCK PGITVDENVE LNKVILRCRA VSSGDSRNSD VIYKLTASGG
PGNKAESKFR QFNKFENGNE WVEVVIMEGL DYEQVNNYTL TLTATDMTSR VASTKTFVVE
VRDVNDVVPQ FTVDLFTGTI DEEMTPNEHL EKTNGKPIVT VKAIDTDSDG PQNEVHYRIV
GEANGEETKH FRIDELTGEI FPNEKFDREK IDMYILTVEA SDRSVSALPG ANGPNKDNVK
VQIVINDVND NAPSFEEQKY IGRVKESEGE GHDVITIKAH DLDKHSNLRY HLIGAGGGRI
PFGVRTDSGT IFVKEPLDFE ASDQYHLVLI ASDGRHNATT NVYIHIEDVN DNAPQFEQQK
YATTVIEEDV DIPKVLFNVH ATDADQDEKS SRIVYRLEGQ GADEVFRIGK YSGTIELVKA
LDRDPPAGVP SWNFVVQAID DDGNGLVGYA DVQVNVRDIN DNSPIFPERL FGYIEENREP
IHSDGVYFMD VQARDFDDPT TENANIEYGI VRNKLINGES VFRIDQNTGK IFAMRSLDRE
ISSEREFIIE VRANDRGVPS REGFANVTIK VTDMNDNAPF FEKTRYEGSV EETAPIGAAV
MSFSAFDADE EAKDNVFTYQ LSEESDYFYV TTDKDSKQSS VGVLRVKQPL DYEDVTQRDG
FHLGIRVSDG RHDAEAAVHV ALVDRNDHAP HIHGATEHRV REDVPRGTSI GRYTATDRDA
GDTARFRINR QSDPKRQFTI DQDGTLRVAH TLDREDIAVY NLIIEAYDNS NNIGRQMVAV
YLQDVNDNGP EPYTVPRPCI FRENTPVNQL GTCEIRATDR DTAEFGPPFT MEVSPSFKYS
QYLNVIFNAN GDGGNGSMTI TPLQEFDREA PVPGKILEIP LILADRAGRR NEASVHVIIG
DLNDNTMHDG RMTIHVNSYL GRLKETVIGR VYVDDADDWD LGDKTFSWKD SRPGFELSDK
GSITMAGEMA AGTYTMSANV HDNARDEDAV GYVTVIVNAV PQIAFDNQGS VQLLIAEETP
LQLPDDFIRA DSNGQSLMDT FKQEMTAYMG GDVTVDVFSV QVGIATLQTR DVPVLNVRFN
ARGSTYRDTA QLNGLIAAHR ADLQRKLNVE IVGVGIDMCK FTQCDAGCQT LNSADYDGIV
VSANSTVIVG VNATSRDDCT CPVWRAPPAC QHSLCHNDGV CHNTNPGFFC ECRNDGLKGA
RCQGTTRSFG GNGFAWYKPM PACTSLNISF SFMTTQSDAL LFYNGPLETL RNDTHIEYSD
YIFIQLRGGR ISLEVSMNGQ SRSSLEVAST ALNDGTWHDI SVNQEGKRVE LVVDNCRFLG
AGADDSSCRA ELYTPDDDER LNIVTPVQIG GLAPLSGQDY PQTIPRAGLN GCVRNLNVNG
DQYDLATPAF EQNSEKGCRL WGATCDSNSV DSLNHCIHGD CFADVQGSGA MVAKCVCDPG
WGGARCERRM EWIQFAQGAF IEYSPRIAFP EQVSDIELLF ISGKVNGAPA ELSFGTDSQQ
SYVSTNLESG QNGVTAAGKF DIGTGGRRAR QELRVSEVLL KENASYWLQF TRNPTRASLS
IDNAYTVSTQ LDKGEPFSLQ VNQITLGTQG QNKGFQGCIG TYRWSKQNLP LKRGGAMDEN
EESIVSISNM AGVQDGCDLR ITCADLPAGY CGGSFVCVDF WKGPFCTCND GANAILGDDG
QVVGCGETLA VSKLGISSPA IILILVSLAL LILLVMMMVV YTRRSPGAFE NVRPEEMNRD
NLRQYGVEGG GEADNDQYSM AGLRKPVMPL DTGMGPAIGG HPPHYPPRGM APPKDDHELN
SKIKDLETDQ NAAPYDELRI YDDERDNISV VTLESIESAQ
