ROL3_CAEEL
ID ROL3_CAEEL Reviewed; 2481 AA.
AC Q8I7I5; D7SFL6; Q8I7I3; Q8I7I4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein roller-3;
DE Flags: Precursor;
GN Name=rol-3; ORFNames=C16D9.2;
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 [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 [2]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17249038; DOI=10.1093/genetics/95.2.317;
RA Cox G.N., Laufer J.S., Kusch M., Edgar R.S.;
RT "Genetic and phenotypic characterization of roller mutants of
RT Caenorhabditis elegans.";
RL Genetics 95:317-339(1980).
RN [3] {ECO:0000305}
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=1752418; DOI=10.1093/genetics/129.3.735;
RA Johnsen R.C., Baillie D.L.;
RT "Genetic analysis of a major segment [LGV(left)] of the genome of
RT Caenorhabditis elegans.";
RL Genetics 129:735-752(1991).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=8138151; DOI=10.1093/genetics/136.1.129;
RA Barbazuk W.B., Johnsen R.C., Baillie D.L.;
RT "The generation and genetic analysis of suppressors of lethal mutations in
RT the Caenorhabditis elegans rol-3(V) gene.";
RL Genetics 136:129-143(1994).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1673, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Thought to have a role in developmental establishment of
CC posterior morphology. {ECO:0000269|PubMed:1752418,
CC ECO:0000269|PubMed:8138151}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255, ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000255, ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed between approximately 30-70 hours after
CC egg lay at 15 degrees Celsius and between 15-35 hours after egg laying
CC at 25 degrees Celsius relating to mid-L1 to mid-L3 stage of larval
CC development. {ECO:0000269|PubMed:8138151}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a larval lethal phenotype,
CC survivors show a rolling phenotype in adults, a locomotive defect.
CC {ECO:0000269|PubMed:17249038, ECO:0000269|PubMed:8138151}.
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DR EMBL; FO080568; CCD64743.1; -; Genomic_DNA.
DR RefSeq; NP_001256097.1; NM_001269168.1.
DR AlphaFoldDB; Q8I7I5; -.
DR SMR; Q8I7I5; -.
DR BioGRID; 44246; 3.
DR IntAct; Q8I7I5; 1.
DR MINT; Q8I7I5; -.
DR STRING; 6239.C16D9.2; -.
DR iPTMnet; Q8I7I5; -.
DR EPD; Q8I7I5; -.
DR PaxDb; Q8I7I5; -.
DR PeptideAtlas; Q8I7I5; -.
DR PRIDE; Q8I7I5; -.
DR EnsemblMetazoa; C16D9.2.1; C16D9.2.1; WBGene00004395.
DR GeneID; 179204; -.
DR KEGG; cel:CELE_C16D9.2; -.
DR UCSC; C16D9.2c; c. elegans.
DR CTD; 179204; -.
DR WormBase; C16D9.2; CE44893; WBGene00004395; rol-3.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000171611; -.
DR HOGENOM; CLU_000848_0_0_1; -.
DR InParanoid; Q8I7I5; -.
DR OMA; STDYKFW; -.
DR OrthoDB; 203310at2759; -.
DR PhylomeDB; Q8I7I5; -.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR PRO; PR:Q8I7I5; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004395; Expressed in embryo and 2 other tissues.
DR GO; GO:0031252; C:cell leading edge; IDA:WormBase.
DR GO; GO:0071944; C:cell periphery; IDA:WormBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..2481
FT /note="Protein roller-3"
FT /id="PRO_0000409663"
FT TOPO_DOM 26..1889
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1890..1910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1911..2481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 617..717
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1046..1143
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1443..1540
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1544..1658
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1665..1768
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1775..1881
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1966..2235
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 2243..2330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2350..2385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2425..2481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2248..2271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2360..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2425..2444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1972..1980
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2001
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1087
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2481 AA; 276238 MW; 53DB9EF286C0F6B7 CRC64;
MLSLHLRSLA ILFLLFFLLH DVVKSATVFS SSLKTCQSQC EERNLAYPLD SGEVHWTGLA
EYNYSSRISS CRHGCEDVDE RESKCDVKCS EEGIVSNACK QGCRAVLVSF LAQAQALLIQ
VHVNMEVLET SMKLKWEFPE TLAEELKEIA NADIFWFSQT KPLNGILGWR WTSLPQNSFR
NSSLSSEVHV PFEHGEHVEV RLALSYRNQV LVSRTTTYHL PLSKSGTTLE VIGQLQLSDD
RVAVCYRTNQ PTPKFKLTIM TLNDNTINTE ESIARCHLFS NLPRDNCCKA SISAIDEHGA
TTAFVEIKLD FYVNQVEIEL VSVASSRLIF SNGTHLLESE IDQYALGDSA TVIPFPLPTD
DTITAIAGIS DTTIAIGSSK GSLWTYQMSA NQTDEDQPSS VIQLKTVGEM DTKINQIEID
HIQRTLYAVQ HDKGIIRCKL RTMEAEESPN CVLIVNNDAL NAPKEITLDS VNGHVYTLNA
DNKVYRTEMV AFNATGIETV ASLQYLQDMS PSNGIFFDVS KFLLYSALQN GSMMTLNPVT
DHVHIFKDVG YADIQHFRIK NDLIYWMKKK CGETDADENC IFAENLQRSE EDIPNKFTYS
SSLMSFGVLE EILLKPRITA VSTIAMLTSD KTARVSWDES NTLPFQAQGS SWRNFTYFLK
VTAPDITDFS PIEIYTSNTE MKIDVTPGNI YNAQVQVCSD DFCSIPTSTS NTALPDLGDV
VPFVFTKRQA DDIISVDILG NIIPADDSVK IVEKLQYPHV LDNTTKTVYL AGDHSMGIFK
KYLDDTAGLP KPFKDGLFVE MMSIMPARSI ILIASSYKIT SYRLPTTFDF EYFSCEEPLE
ACSEVMGISS DDTTGMVHFL TQARNGTITL WESDPENRTP RDIASVPSIV PFRRFLILHD
KMILVTKNNH IVQTDKKLKV VNVATELERV DHILPLRYAT ISHKIEFSDE IKFIDGSKTN
LQWTLSPPLE AGTVLFKVSI FREKMGGQDP PIITIQSETN FTIPSEVLEA WSSAQRFDVS
VQAMTPWATA VLNRTGLTAP VKPPTSPTQL RIFATQQKTV DGPRALISFF WGPPSEWNGT
PYQYIVNCTK DDGSWIGGPV TTSQSHYSFA VKSGKVSCQA AAANEPTNIG SFSELITIDS
SELKPLVKLF AIDSTNSLIS INDLAHEEPR RETRQVAQPV KLEYQAMAFI GEDLYAVRKE
GESAQPVLVQ IDTNHIDNTV HKVSIGGDVT RIDAMTSDWV GNRLIFVAGT NVYQLSLEPF
LSTSLLNPHK LIQLTSATDA KQLAYDPFMN TAYLLTKNGS LFALDMNKNT EANLALTVSC
LASQTVTWMM TEFAWNRASS PKIYALTWNG LIYVDLTEDS QCNEVRIDWT KFGDKGLKDI
SSFAIADKLF AFVTSSEMLI YGKDTVTPIT IANPPLKQIL AVSQSSQPYP ERSCFELPSS
KGIVFSIVNE GKTGSFLEVT KSSSSSSCQE VSMPQTQYEI YFTRKNTDKV KHVRSFSDRI
HVENGILDKE TDYDVTVTWL NRYSPASGVS ASKSFRTGFG YPSAPRDPHA IPVTPDTVYL
YWNLPETLNA PISEIKYKIS QQAAGISVPT SIAVIALSET VSSNISSDTT SCLINPCRVK
IANLRPSNEY KFWVTATHIS HLDAATILKD DDAVSSEAVA RTLDVPGTLR PDNVTGSSLL
LRWNGLEPEH RPSSIAVQYR ESGGANNEWQ FPMNVSFEPD VTTELVPITN LLSATSYDYR
FVATYTGTYT IDGKVLAFKE DYLQLPQQAR TKAGVPTAPQ FVEAKQDEEG WIVTWKEPMS
DGGSPITSYA VETRINKTAE WEIAERGLDG WKTWWRPGKS DTTSSTSTSS TEVSEFRIRA
ANIEGFGAYA YTEDKKEEKE EEPSSVLPYL LLLSIIFLLA AMILVACFWL KSRRRQQQKK
REAEDERNCI RLDVVANMNF SSSHQSLPPE YESEMRNLPV VNYSTVTFND YIDTCAYGIV
HSGTAEEVPM SWEKDVRVAI KKLKPNHSFQ EKMMFMKEAI LLNNLDHPNI VKELGVCITP
GQELILLEYM EGGNLLKFLQ KSTPNEYQSS ELSPRDLLSI SVDIARGMNY LERLPHVHKN
LSARKCLLAG RPGVTKLEMG MSKELSNGQV NRSDLENMEI VRWMAPEVLK DFQFSSKSDV
WAYGVLLYEV FSFGEVPYGD KDNRRIMTDV RNGSVLPIPS YCPSKRIYKV IKQCLTSDST
KRANFATILK IFETFRDDQK CQDDKPIQFN DGTDNTNFSA SQDSTSSREP PSPSHRMRDF
IDTRDLEPPS PSHLNQSFGG FEHPYEGERP ATMWNGSGAR NSAKNSIGRS MKKEKLRNPI
HSMDDLVARN QRPLSIHSED TESTDYGASS SMYSPGSSNR ISSQVDPPIG RLSSAPGIGI
VNDAFESSNP SLNLSRSWAG LSREVNQNPA GAGSSGTLPQ HTNSAGHLRL PGVQVGAGGG
RVYRNASGGG GPSNRGRISQ V
