ROL3_CAEBR
ID ROL3_CAEBR Reviewed; 2439 AA.
AC Q61G93; A8XDA6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein roller-3;
DE Flags: Precursor;
GN Name=rol-3 {ECO:0000250|UniProtKB:Q8I7I5}; ORFNames=CBG11320;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Involved in larval development and locomotion.
CC {ECO:0000250|UniProtKB:Q8I7I5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255, ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000255, ECO:0000305}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255}.
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DR EMBL; HE600908; CAP30625.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61G93; -.
DR SMR; Q61G93; -.
DR STRING; 6238.CBG11320; -.
DR WormBase; CBG11320; CBP37602; WBGene00032454; Cbr-rol-3.
DR eggNOG; KOG1095; Eukaryota.
DR HOGENOM; CLU_000848_0_0_1; -.
DR InParanoid; Q61G93; -.
DR OMA; STDYKFW; -.
DR OrthoDB; 203310at2759; -.
DR Proteomes; UP000008549; Chromosome V.
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; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; ISS: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; 3.
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; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..2439
FT /note="Protein roller-3"
FT /id="PRO_0000312666"
FT TOPO_DOM 27..1851
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1852..1872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1873..2439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 618..720
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1403..1503
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1507..1628
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1629..1732
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1738..1843
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1928..2199
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 2214..2277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2315..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2412..2439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2216..2235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2325..2348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2420..2439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1934..1942
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1963
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2439 AA; 271800 MW; 68E8D1F75C448040 CRC64;
MLDFPRFSLF LFLLFSSFLF SSFVHAATVF SSSLKTCQSQ CEERNLAYPL DSGEVHWTGL
AEFNYTTRIS SCKHGCEDVD ERESKCNVKC AEEGIVTNSC KQGCRAVLVS FLAQAQALLI
QTRVNMEVLE TAMKLKWEFP ETLAEELKEI ANADIFWFSQ TRPLNGILGW RWTSLPQSSF
RNSSLVSEVH VPFEHGEHVE VRLALSYRNQ VLVSRTTTYH LPLSKAGTTL EVIGQLQLSD
DRVAVCYRTN QPTPKFKLTV MTMDDNTINT EESISRCHLF SNLPRDNCCK ASISAIDEHG
ATTAFVEIKL DFFVNQVEIE LVSAASSSRI IFSNGTHLLE NEELAQYALG DSATVIPFPL
PTDDTITAIA GITDTIIAIG SSKGSLWTFQ MSANQTDEDQ PSSVIQLKTV GEMDTKITQI
EIDHIQRTLY AVQHDKGILR CKLRTMESEE SPTCVLIVNN DALNPPKEIT LDPVNGHIYS
LNVDNKVYRT EMIAFNATGI ETVASLQYLK DMSPSNGIFF DVSKFLLYSA LQNGSMMTLN
PVTDQAHIFK DSGYTDVQNF RIKSDLIYWM KKKCGKTDAD ENCIFTENLQ RSEEDIPNKF
TYSSALMSYS FLEEILLKPR IVAVSSIALL TSDKTGRVSW DEANTLPFQA QGSSWRNFTY
FLKITAPDIT DFEAVEMYTS STDVKIDVTP GNQYNAQVQV CSDDFCSTPS STSNTALPDL
GGGVPFVFTK KKADDIISID MLGNLVITDD SVKAVERMQN PHVLDNTTKT VYLAGDHSMG
IFKKDLDDAT GSPKPFKDGL FVEMMSIMPS RSMILIASSY KITSYRLPTT FDFEYYSCEE
PLEDCAEVMG ISSDDSTGMV YFLTQSRNGT VILWESDPEN RAPRDIATAP SIVPFRRFLI
IHDKMILVTK NNHIVQTDKS LKVVNVATEL ERVDRILPLR YAAISHKIEF TDEIKFMEGS
KTDLQWTLSP PLEAGTVIFK VSFFREKMGG QDAPITTIQS DTNFTIPPEV LKEWSSAQRF
DVSIQAITPW ATAVLNRTGL TAPVKPPTPP TQLKIFATQQ KTVDGPRALI SFFWGPPLEW
NGTPYQYIVN CTKDDGKVIT IDSSELKPLV KLFAIDSTNS LIIINDLAHE EPRRETRQVT
QPVKLDYQAM AFIGEDLYTV RKEGESAQPF LVQIDTNHID NTVHKVSIGG DVTRIDAMTS
DWVGNRLIFV AGTNLYQLSL EPFLSTSLLN PHKLITLSAA TDAKQLAYDP FMNTAYLLTK
NGSLFALDMN KNTEANLALT VPCLASQTVT WMMTEFAWNR ASSPKIYALT WNGLINVDLA
EDFQCNEVRI DWSKFGEKGL KAISSFAIAD KLFAFVTSSE MLIYGRDTVT PITIANPPLK
QILAVSQSSQ PYPERSCFEL PSSKGIVFSI VNEGKTGALL EVTKSSSSSA CLDVSMPQTQ
YEIYFTRKNT DKVKHVRSFS DRIHVENGIL DKETDYDVTV TWLNRYSPAS GVSSSRSFRT
GFGYPSAPRD PHAIPVTPDT VYLYWSLPET LNAPISEIKY KISQQAAGIS VPTSIAVIPL
SETVSSNISS DTTACLINPC RVKIANLRPS NEYKFWVTAT HISHLDAATI LKDDDAVSSE
AVARTLDVPG TLRPDNVTGS SLLLRWNGLE PEHRPTSIAI QYRESGGANN EWQSPTNASF
EPDVATELVP VTNLLSATTY DYRFVATYTG TYTIDGKVLA FKEDYLQLIQ QARTKAGVPT
APQSVEAKID TEGWIVTWKE PMSDGGSPIT SYAVETRINK TAEWEIAERG LDGWKTWWRP
GKSETSSSMS YSSEVSEFRI RAANIEGFGA YAYTEEKKEE KEEEKGGILP YFLGISIILL
LAAMILVGCF WLKSRRRQQM KKREAEDERN CIRLDVVANM NFTNSRQTLS PEYESEIRNL
PIVDYNDVEI VRHISDCSYG SVHEGIAEEV PLSWEKQVKV AVKQLRPKSA NHDFDRMMFM
KEAILLNNLD HNIVKELGVC VSPGQGLILL EYMEGGNLLN FLRESAPSEM QASELSTRDL
LAISVDIARG MNYLERLPHV HKNLSARKCL LSGRPGVAKL EMGMPRALSK GEINRVDLES
MQSVKWMAPE VFKDLMFTSK SDVWAYGVLL YEIFSFGEEP YGSMDSRRVI TDVRDGNLTL
PVPPYCPSKK ICKVMKMCLI SDPNKRASFA TILKIFETCR DDQQSQDDKR IHFNEGSDNI
NFNASQDSTS SREPPSPSHR IREFTQISGD LEPPSPSPLN QSFGGFEHPY EGDRPATMWN
ASGARNSAKN SIGRSMKKDK FRNPIHSMDD LVARSQRPLS IHSEDTESTD FGGATSSMHS
PSSSNRTNHY ELPMSRLSAA PPIGIVNNAF ESSNNSLNMS RSWTGLAGEV NPNPAGASSS
GTLPHHANSM VHLRAPTGQP PTRVNRNSSG GTCRSVSQV
