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Protein

ALK tyrosine kinase receptor homolog scd-2

Gene

scd-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable tyrosine-protein kinase receptor which regulates the dauer/non-dauer developmental decision probably by controlling daf-3 transcriptional activity in parallel or together with the TGF-beta pathway (PubMed:11063683, PubMed:18674914). Regulates integration of conflicting sensory cues in AIA interneurons (PubMed:21414922). May act as a receptor for hen-1 (PubMed:18674914, PubMed:21414922).3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1003 – 10031ATPPROSITE-ProRule annotation
Active sitei1106 – 11061Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi982 – 9909ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • chemotaxis Source: UniProtKB-KW
  • dauer larval development Source: WormBase
  • sensory perception of chemical stimulus Source: UniProtKB
  • sensory processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Chemotaxis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ALK tyrosine kinase receptor homolog scd-2Curated (EC:2.7.10.1Curated)
Alternative name(s):
Suppressor of constitutive dauer formation protein 2Imported
Gene namesi
Name:scd-2Imported
ORF Names:T10H9.2Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiT10H9.2; CE45495; WBGene00004740; scd-2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 903883ExtracellularSequence analysisAdd
BLAST
Transmembranei904 – 92421HelicalSequence analysisAdd
BLAST
Topological domaini925 – 1421497CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1174 – 11741G → E in sa249; moderate decrease in dauer formation. Partially suppresses constitutive dauer formation in mutants of the TGF-beta pathway. Defect in sensory integration when confronted to two opposing environmental chemicals. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 14211401ALK tyrosine kinase receptor homolog scd-2CuratedPRO_0000434037Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi44 – 441N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi70 – 701N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi83 – 831N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi119 – 1191N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi201 – 2011N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi301 ↔ 317PROSITE-ProRule annotation
Disulfide bondi309 ↔ 329PROSITE-ProRule annotation
Disulfide bondi323 ↔ 338PROSITE-ProRule annotation
Glycosylationi342 – 3421N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi362 – 3621N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi495 – 4951N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi533 – 5331N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi546 – 5461N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi633 – 6331N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi726 – 7261N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi793 – 7931N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi849 – 8491N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi873 – 8731N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi893 – 8931N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO76411.
PRIDEiO76411.

Expressioni

Tissue specificityi

Expressed in AIA sensory neurons.1 Publication

Interactioni

Subunit structurei

Interacts (via cytoplasmic domain) with fsn-1 (via SPRY domain).1 Publication

Protein-protein interaction databases

STRINGi6239.T10H9.2.

Structurei

3D structure databases

ProteinModelPortaliO76411.
SMRiO76411. Positions 894-1314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini300 – 33839LDL-receptor class APROSITE-ProRule annotationAdd
BLAST
Domaini339 – 542204MAMPROSITE-ProRule annotationAdd
BLAST
Domaini976 – 1261286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 LDL-receptor class A domain.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1095. Eukaryota.
ENOG410XPVX. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000021502.
InParanoidiO76411.
OMAiNEEVMLM.
OrthoDBiEOG7GN2KT.

Family and domain databases

InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50068. LDLRA_2. 1 hit.
PS50060. MAM_2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O76411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRRLWWFV VLFRVTLVGA ILPNETFDVR RYYADRFLIE DEENGSSRSY
60 70 80 90 100
YISAESKAKA AEQFALLAPN CSLTSDIQEN TCNETSSFCD HRVDSTYKTY
110 120 130 140 150
HYEQEKCNCF IETCDEETNS TELMVLYPDC YCGKREKHCD LSKEKCHWTP
160 170 180 190 200
DSDHDDLKFE VFESSNKVLF DYMLQAGSEK ANLKMNKVSM VSKFFRQSGF
210 220 230 240 250
NCSLRFMHHF THQSSTSRLV VRSILQSGEK KNLYEHWLKP ASVFWVPVQV
260 270 280 290 300
AIGSYAEPFK ISIDCETGFP PKKKKNKPFT CSIADIYFEN CGEIRDPIEQ
310 320 330 340 350
CSRGDQFLCS ISANTRCLQN AQCDSRIDCD DESDEMDCGN INGTMCDFNG
360 370 380 390 400
QDYCNSWYQV TNVTDYHERL SEPTTVAPLN KLNEVPLHLF RLQSPSAKIK
410 420 430 440 450
EAMRGSGNML VFDHKPNPLT RRTSALVSPE LPRTNPEAYD EKSPLFKSCK
460 470 480 490 500
LRFYLCSRTY SKVWQISVIS KGINPMESGR TIIYEAGYTL IPKENCTWER
510 520 530 540 550
VFVNIPRQNA GFRIGIFVTN YFPGSEEYVA IDNLSFSPTC FERDINQSTW
560 570 580 590 600
DIPDLFINTC GASGFEQPQN CDHNRELDGQ TGHFLKEDGT QQWTVPVTGF
610 620 630 640 650
YRMEICGAGG GSNSKASGDT GDCVTLQVHL IENLSLRMLI GQMGESPCFT
660 670 680 690 700
EHDDELRPSS CSKISHNYVY DGKRGAAGGG ATLLTVEKDL WNVVAGGGAG
710 720 730 740 750
ASWDGFDMEV GYGASAIHVK PDQRCNETCK AVSHTDFIVE RRDNRCPGEK
760 770 780 790 800
GESTVFGGFG GGGNSCGMLG GSGAGYQAGN PFGKSRARSG SSNVSIDFSK
810 820 830 840 850
SPIYYQSERL DEGYIKIAFC RKRCEPPTVC RFRKDYFEEE YCGCPDGSNV
860 870 880 890 900
TDTEEACAFP LVCPSSSTNQ YRNFTYEPFC LCNNGKEIYD VYNDTCEEIQ
910 920 930 940 950
IWTLYNITFL IFAALTIIGA LFVVYHYRNR EKQMKQEILD LTQMKSPDYL
960 970 980 990 1000
YDDIYFGRTT RKAALDSLPS ISRDSIERGR VLGRGNFGEV YYGEYSGVKL
1010 1020 1030 1040 1050
AVKMISRTFS ASQASQSDFC NEALCMGTFV DENVVRLIGI DFEKVPYMIA
1060 1070 1080 1090 1100
LEYMEGGDLL SFVKECRPNQ VSLNPFQLAM SDLIKICCDV AAGCKCLETF
1110 1120 1130 1140 1150
GYVHRDIAAR NILLTTRGPQ RVAKIADFGM AKEITYGTEY YRINGRTMMP
1160 1170 1180 1190 1200
IKWTPPEAFI DGVFTTKSDI WSFGVLCWEV FSLGVVPYPN RRNEEVMLML
1210 1220 1230 1240 1250
TEGARLEYPY GIPTRVYQLM RDCWKTAAAD RPKFVDVVEI FQDIQDDPAS
1260 1270 1280 1290 1300
VGMPFPIHPA VRATFAHSQS TPVSVETPMT AMTEISLNST FTDASTVKVS
1310 1320 1330 1340 1350
AQQDMQDRIQ LHELMLTREH PYTSELTSYV VNSIRKDLAR VQYENGLTSV
1360 1370 1380 1390 1400
PQPEYLSPEN NDESVQLIPQ SNTVTDQTPP TSLIDLNRLG VQNTGPTLHR
1410 1420
PDSLNFNDPY SSVPLLECQT R
Length:1,421
Mass (Da):160,425
Last modified:January 11, 2011 - v3
Checksum:iC32F31F103D48041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284605 Genomic DNA. Translation: CCD71218.1.
RefSeqiNP_504685.3. NM_072284.3.
UniGeneiCel.5331.

Genome annotation databases

EnsemblMetazoaiT10H9.2; T10H9.2; WBGene00004740.
GeneIDi179054.
KEGGicel:CELE_T10H9.2.
UCSCiT10H9.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284605 Genomic DNA. Translation: CCD71218.1.
RefSeqiNP_504685.3. NM_072284.3.
UniGeneiCel.5331.

3D structure databases

ProteinModelPortaliO76411.
SMRiO76411. Positions 894-1314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.T10H9.2.

Proteomic databases

PaxDbiO76411.
PRIDEiO76411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT10H9.2; T10H9.2; WBGene00004740.
GeneIDi179054.
KEGGicel:CELE_T10H9.2.
UCSCiT10H9.2. c. elegans.

Organism-specific databases

CTDi179054.
WormBaseiT10H9.2; CE45495; WBGene00004740; scd-2.

Phylogenomic databases

eggNOGiKOG1095. Eukaryota.
ENOG410XPVX. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000021502.
InParanoidiO76411.
OMAiNEEVMLM.
OrthoDBiEOG7GN2KT.

Miscellaneous databases

NextBioi903708.
PROiO76411.

Family and domain databases

InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR002172. LDrepeatLR_classA_rpt.
IPR000998. MAM_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00192. LDLa. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50068. LDLRA_2. 1 hit.
PS50060. MAM_2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  2. "Suppressors of transforming growth factor-beta pathway mutants in the Caenorhabditis elegans dauer formation pathway."
    Inoue T., Thomas J.H.
    Genetics 156:1035-1046(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-1174.
  3. "An SCF-like ubiquitin ligase complex that controls presynaptic differentiation."
    Liao E.H., Hung W., Abrams B., Zhen M.
    Nature 430:345-350(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FSN-1.
  4. "C. elegans anaplastic lymphoma kinase ortholog SCD-2 controls dauer formation by modulating TGF-beta signaling."
    Reiner D.J., Ailion M., Thomas J.H., Meyer B.J.
    Curr. Biol. 18:1101-1109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-1174.
  5. "Behavioral choice between conflicting alternatives is regulated by a receptor guanylyl cyclase, GCY-28, and a receptor tyrosine kinase, SCD-2, in AIA interneurons of Caenorhabditis elegans."
    Shinkai Y., Yamamoto Y., Fujiwara M., Tabata T., Murayama T., Hirotsu T., Ikeda D.D., Tsunozaki M., Iino Y., Bargmann C.I., Katsura I., Ishihara T.
    J. Neurosci. 31:3007-3015(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-1174.

Entry informationi

Entry nameiSCD2_CAEEL
AccessioniPrimary (citable) accession number: O76411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: January 11, 2011
Last modified: March 16, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.