SCD2_CAEEL
ID SCD2_CAEEL Reviewed; 1421 AA.
AC O76411;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=ALK tyrosine kinase receptor homolog scd-2 {ECO:0000305};
DE EC=2.7.10.1 {ECO:0000305};
DE AltName: Full=Suppressor of constitutive dauer formation protein 2 {ECO:0000312|WormBase:T10H9.2};
DE Flags: Precursor;
GN Name=scd-2 {ECO:0000312|WormBase:T10H9.2};
GN ORFNames=T10H9.2 {ECO:0000312|WormBase:T10H9.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-1174.
RX PubMed=11063683; DOI=10.1093/genetics/156.3.1035;
RA Inoue T., Thomas J.H.;
RT "Suppressors of transforming growth factor-beta pathway mutants in the
RT Caenorhabditis elegans dauer formation pathway.";
RL Genetics 156:1035-1046(2000).
RN [3] {ECO:0000305}
RP INTERACTION WITH FSN-1.
RX PubMed=15208641; DOI=10.1038/nature02647;
RA Liao E.H., Hung W., Abrams B., Zhen M.;
RT "An SCF-like ubiquitin ligase complex that controls presynaptic
RT differentiation.";
RL Nature 430:345-350(2004).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-1174.
RX PubMed=18674914; DOI=10.1016/j.cub.2008.06.060;
RA Reiner D.J., Ailion M., Thomas J.H., Meyer B.J.;
RT "C. elegans anaplastic lymphoma kinase ortholog SCD-2 controls dauer
RT formation by modulating TGF-beta signaling.";
RL Curr. Biol. 18:1101-1109(2008).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-1174.
RX PubMed=21414922; DOI=10.1523/jneurosci.4691-10.2011;
RA Shinkai Y., Yamamoto Y., Fujiwara M., Tabata T., Murayama T., Hirotsu T.,
RA Ikeda D.D., Tsunozaki M., Iino Y., Bargmann C.I., Katsura I., Ishihara T.;
RT "Behavioral choice between conflicting alternatives is regulated by a
RT receptor guanylyl cyclase, GCY-28, and a receptor tyrosine kinase, SCD-2,
RT in AIA interneurons of Caenorhabditis elegans.";
RL J. Neurosci. 31:3007-3015(2011).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ALA-1001 AND GLY-1174.
RX PubMed=28924007; DOI=10.1523/jneurosci.0031-17.2017;
RA Kitazono T., Hara-Kuge S., Matsuda O., Inoue A., Fujiwara M., Ishihara T.;
RT "Multiple Signaling Pathways Coordinately Regulate Forgetting of Olfactory
RT Adaptation through Control of Sensory Responses in Caenorhabditis
RT elegans.";
RL J. Neurosci. 37:10240-10251(2017).
CC -!- FUNCTION: Probable tyrosine-protein kinase receptor which regulates the
CC dauer/non-dauer developmental decision probably by controlling daf-3
CC transcriptional activity in parallel or together with the TGF-beta
CC pathway (PubMed:11063683, PubMed:18674914). Regulates integration of
CC conflicting sensory cues in AIA interneurons (PubMed:21414922). May act
CC as a receptor for hen-1 (PubMed:18674914, PubMed:21414922). In AWA
CC neurons, together with hen-1, plays a role in regulating olfactory
CC adaptation by controlling the forgetting sensory responses to odorants
CC such as diacetyl (PubMed:28924007). {ECO:0000269|PubMed:11063683,
CC ECO:0000269|PubMed:18674914, ECO:0000269|PubMed:21414922,
CC ECO:0000269|PubMed:28924007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with fsn-1 (via SPRY
CC domain). {ECO:0000269|PubMed:15208641}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in AIA sensory neurons.
CC {ECO:0000269|PubMed:21414922}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000305}.
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DR EMBL; BX284605; CCD71218.1; -; Genomic_DNA.
DR RefSeq; NP_504685.3; NM_072284.3.
DR PDB; 7LIR; X-ray; 2.60 A; A/B=549-898.
DR PDBsum; 7LIR; -.
DR AlphaFoldDB; O76411; -.
DR SMR; O76411; -.
DR IntAct; O76411; 1.
DR STRING; 6239.T10H9.2; -.
DR PaxDb; O76411; -.
DR PeptideAtlas; O76411; -.
DR EnsemblMetazoa; T10H9.2.1; T10H9.2.1; WBGene00004740.
DR GeneID; 179054; -.
DR KEGG; cel:CELE_T10H9.2; -.
DR UCSC; T10H9.2; c. elegans.
DR CTD; 179054; -.
DR WormBase; T10H9.2; CE45495; WBGene00004740; scd-2.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000174242; -.
DR HOGENOM; CLU_253074_0_0_1; -.
DR InParanoid; O76411; -.
DR OMA; NEEVMLM; -.
DR OrthoDB; 128386at2759; -.
DR PhylomeDB; O76411; -.
DR PRO; PR:O76411; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004740; Expressed in larva and 2 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IMP:UniProtKB.
DR GO; GO:0050893; P:sensory processing; IMP:UniProtKB.
DR CDD; cd00112; LDLa; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Chemotaxis; Disulfide bond;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1421
FT /note="ALK tyrosine kinase receptor homolog scd-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434037"
FT TOPO_DOM 21..903
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..1421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 300..338
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 339..542
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 976..1261
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 982..990
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1003
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 301..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 309..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 323..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT MUTAGEN 1001
FT /note="A->T: In qj141; defective olfactory adaptation
FT resulting in impaired forgetting sensory responses to the
FT odorant diacetyl."
FT /evidence="ECO:0000269|PubMed:28924007"
FT MUTAGEN 1174
FT /note="G->E: In sa249; moderate decrease in dauer
FT formation. Partially suppresses constitutive dauer
FT formation in mutants of the TGF-beta pathway. Defect in
FT sensory integration when confronted to two opposing
FT environmental chemicals. Defective olfactory adaptation
FT resulting in impaired forgetting sensory responses to the
FT odorant diacetyl."
FT /evidence="ECO:0000269|PubMed:11063683,
FT ECO:0000269|PubMed:18674914, ECO:0000269|PubMed:21414922,
FT ECO:0000269|PubMed:28924007"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 597..606
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 682..690
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:7LIR"
FT HELIX 727..732
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 735..738
FT /evidence="ECO:0007829|PDB:7LIR"
FT TURN 741..744
FT /evidence="ECO:0007829|PDB:7LIR"
FT HELIX 748..753
FT /evidence="ECO:0007829|PDB:7LIR"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 765..769
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:7LIR"
FT HELIX 785..788
FT /evidence="ECO:0007829|PDB:7LIR"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 814..819
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 829..832
FT /evidence="ECO:0007829|PDB:7LIR"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 840..843
FT /evidence="ECO:0007829|PDB:7LIR"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 853..855
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 865..871
FT /evidence="ECO:0007829|PDB:7LIR"
FT TURN 873..875
FT /evidence="ECO:0007829|PDB:7LIR"
FT STRAND 878..882
FT /evidence="ECO:0007829|PDB:7LIR"
SQ SEQUENCE 1421 AA; 160425 MW; C32F31F103D48041 CRC64;
MRKRRLWWFV VLFRVTLVGA ILPNETFDVR RYYADRFLIE DEENGSSRSY YISAESKAKA
AEQFALLAPN CSLTSDIQEN TCNETSSFCD HRVDSTYKTY HYEQEKCNCF IETCDEETNS
TELMVLYPDC YCGKREKHCD LSKEKCHWTP DSDHDDLKFE VFESSNKVLF DYMLQAGSEK
ANLKMNKVSM VSKFFRQSGF NCSLRFMHHF THQSSTSRLV VRSILQSGEK KNLYEHWLKP
ASVFWVPVQV AIGSYAEPFK ISIDCETGFP PKKKKNKPFT CSIADIYFEN CGEIRDPIEQ
CSRGDQFLCS ISANTRCLQN AQCDSRIDCD DESDEMDCGN INGTMCDFNG QDYCNSWYQV
TNVTDYHERL SEPTTVAPLN KLNEVPLHLF RLQSPSAKIK EAMRGSGNML VFDHKPNPLT
RRTSALVSPE LPRTNPEAYD EKSPLFKSCK LRFYLCSRTY SKVWQISVIS KGINPMESGR
TIIYEAGYTL IPKENCTWER VFVNIPRQNA GFRIGIFVTN YFPGSEEYVA IDNLSFSPTC
FERDINQSTW DIPDLFINTC GASGFEQPQN CDHNRELDGQ TGHFLKEDGT QQWTVPVTGF
YRMEICGAGG GSNSKASGDT GDCVTLQVHL IENLSLRMLI GQMGESPCFT EHDDELRPSS
CSKISHNYVY DGKRGAAGGG ATLLTVEKDL WNVVAGGGAG ASWDGFDMEV GYGASAIHVK
PDQRCNETCK AVSHTDFIVE RRDNRCPGEK GESTVFGGFG GGGNSCGMLG GSGAGYQAGN
PFGKSRARSG SSNVSIDFSK SPIYYQSERL DEGYIKIAFC RKRCEPPTVC RFRKDYFEEE
YCGCPDGSNV TDTEEACAFP LVCPSSSTNQ YRNFTYEPFC LCNNGKEIYD VYNDTCEEIQ
IWTLYNITFL IFAALTIIGA LFVVYHYRNR EKQMKQEILD LTQMKSPDYL YDDIYFGRTT
RKAALDSLPS ISRDSIERGR VLGRGNFGEV YYGEYSGVKL AVKMISRTFS ASQASQSDFC
NEALCMGTFV DENVVRLIGI DFEKVPYMIA LEYMEGGDLL SFVKECRPNQ VSLNPFQLAM
SDLIKICCDV AAGCKCLETF GYVHRDIAAR NILLTTRGPQ RVAKIADFGM AKEITYGTEY
YRINGRTMMP IKWTPPEAFI DGVFTTKSDI WSFGVLCWEV FSLGVVPYPN RRNEEVMLML
TEGARLEYPY GIPTRVYQLM RDCWKTAAAD RPKFVDVVEI FQDIQDDPAS VGMPFPIHPA
VRATFAHSQS TPVSVETPMT AMTEISLNST FTDASTVKVS AQQDMQDRIQ LHELMLTREH
PYTSELTSYV VNSIRKDLAR VQYENGLTSV PQPEYLSPEN NDESVQLIPQ SNTVTDQTPP
TSLIDLNRLG VQNTGPTLHR PDSLNFNDPY SSVPLLECQT R
