SDK_CAEEL
ID SDK_CAEEL Reviewed; 2325 AA.
AC Q9N3X8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein sidekick homolog;
DE AltName: Full=Neuronal IgCAM protein 4;
DE Flags: Precursor;
GN Name=rig-4; ORFNames=Y42H9B.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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-932, AND IDENTIFICATION BY MASS
RP 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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-932 AND ASN-1016, AND
RP IDENTIFICATION BY 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: Cell adhesion protein. {ECO:0000250|UniProtKB:O97394}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
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DR EMBL; FO080677; CCD65705.1; -; Genomic_DNA.
DR RefSeq; NP_501339.2; NM_068938.6.
DR AlphaFoldDB; Q9N3X8; -.
DR STRING; 6239.Y42H9B.2; -.
DR iPTMnet; Q9N3X8; -.
DR EPD; Q9N3X8; -.
DR PaxDb; Q9N3X8; -.
DR PeptideAtlas; Q9N3X8; -.
DR PRIDE; Q9N3X8; -.
DR EnsemblMetazoa; Y42H9B.2.1; Y42H9B.2.1; WBGene00004371.
DR GeneID; 177597; -.
DR KEGG; cel:CELE_Y42H9B.2; -.
DR UCSC; Y42H9B.2; c. elegans.
DR CTD; 177597; -.
DR WormBase; Y42H9B.2; CE33870; WBGene00004371; rig-4.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_001875_1_0_1; -.
DR InParanoid; Q9N3X8; -.
DR OMA; EWVVPHK; -.
DR OrthoDB; 134749at2759; -.
DR PhylomeDB; Q9N3X8; -.
DR PRO; PR:Q9N3X8; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004371; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 12.
DR Gene3D; 2.60.40.10; -; 17.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 8.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 12.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..2325
FT /note="Protein sidekick homolog"
FT /id="PRO_0000226982"
FT TOPO_DOM 27..2019
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2020..2040
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2041..2325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 217..319
FT /note="Ig-like C2-type 2"
FT DOMAIN 324..397
FT /note="Ig-like C2-type 3"
FT DOMAIN 456..544
FT /note="Ig-like C2-type 4"
FT DOMAIN 547..638
FT /note="Ig-like C2-type 5"
FT DOMAIN 645..751
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 756..853
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 858..957
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 961..1055
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1059..1154
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1159..1254
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1259..1359
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1363..1457
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1463..1566
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1571..1671
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1673..1775
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1776..1872
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1873..2004
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1036..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2202..2226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2285..2325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2080..2103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2209..2226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2291..2325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
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 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 345..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 480..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 568..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2325 AA; 259165 MW; 6F3E76CA3303338E CRC64;
MRNRLLLIFY TTTVLWTIGY TQLVLGKPPI FQDGGSVEQK VAVEGEIIRL KCDDAELAEQ
YEWRIGDASG ELIATSKFCE VQASRVNDEK KYRCVARNTV GAAISPPSMV RSKYLDDFDA
SDESVQYEVT TGVGRYFVLR RPTLLASRNL DISYSWIKDD SHQVTPDATH FVTSDGNLVV
TGVKRDDFGA YKLMASSDDL KEIVSKEYNV RDNGLSPSLQ NTLSIVYFPT DRTIIESTLP
HDEIFDCVTS FGSKDDVRIR WFLNGQQISG SEVGMTTTLN NRRLIISNPS SFTRGEHKLE
CRADAAMGRT SDQKSAYMTF ISRPILKDLP NEIQKTVGSS LSLKCSVKKK SSMDIKWYKN
GLMMTTQRGK LTIDRIKQDD FGLYQCEATN AAGADLASVW VKEGEANETV ATEMSEDGMS
LEEEISMETP PPRKLKFFDN SKSQEQLFPF TSELEPSQKL IKTPKDLTVA SGTDRIMMEC
AATGSPPPNI IWLLNGHEIQ TDNVKYDLTN DGLAIHDIRK SDEGEYTCEI SGSNVKATAN
VQVNGDSLIE YGPADQKSLI GTNVEFSCEV AKEYVRKASV EWYLNDVLLP VNGNSGLRIS
RNRKGSLIIR QVGPDNTGEY RCRVTVDGRE ENASAMLQII EKPAMPERVR AELHNETMPA
KVRVRWNEGF DGNEPIIKHA IEMRTMGPTG LWSDWTTAID NIPKEEGKPC CWTDIEDLRP
SSTAEFRVVA SNKHGPGKPS LPSYSVTMPQ QPPSAAPRNV AASARSPHSV MVQWQQPKEE
LDSGDVLGYV VRYRLAGYSS LTWNEKNLTT KDARNTLVDE LITWREYEIQ VAAYNKRGLG
VFSESIEVTT SEGRPTQAPK NVRVKVLNST AVAIEFTAPE QQRIPGVNLG YKVQFWKGEP
EKGELYKQVI LDPDRRQLTT VVNELEKFGH YNLTTLCFTT PGDGPRSNVV KVVTEEDTPE
SVDELSIAEV MYNGAVITWN SPLKQNGIVT KYTIRHWAAS SPDVKTKHEV DGSTTNFTID
GLQPSTRYGV DVMASTRKGD GPVEETKFES GVPPELPGRP SMLSIGDISA TTVQLHFTPG
FDGHTAIRQW VVEGKMADSS VFAHVFNVSA PKARSITVTG LRPFTQYQLR LIAENVKGRG
APSEPSRSFE TLQTNPDTPS QRLFAEPVSA TSISVSWTPL LATHWNGQPK GYLIVYREID
DENWKEVRTP ALRSSEHTVT DLRPFTSYEV NVFSENGFGR SLPTDSVKAR TYESVPSGSP
RNIVVTAEGS KAAIIKWNPV AELSTNGDVI GYKLRVVPER ESLMADETKV IDIPGQSTLM
AKVSDLRPFT SYHVYMSAYT IVGNGPENST PISFETMEDV PAPPESFQCS YISEQEVRMK
WLPPGSPNGK ITNYIISYWK SHEPRSMAID APLLGNLLMF AAMSLNPNTQ YTFAIKARNS
KGESEEAVAE VMTSSVRLPV RNAPAPVRDT LSQHQATEII IRWDESLPRK LTEDAESPVR
AVQVSYQKTN EDEWITLEKK FEYSKRRSVI KHLSPNSMFR FRIRFIGDFL ESSWSPESEW
MRTLPSAPFA QPISLKATPY ERNSVQLEWV VPHKSTWNSD AIGYRIHYRE YPSNETWQME
EIAIRDEHED KEEKILAKLD SFKHYILRMR IFNSEGEGPF SAPVFAYVGY SIPKRNLNNI
ITEPLSSSSI RVKWDAWPKE DSETITSFKV RYVPVASVLS SVSSEEEIMI VDTNECTLND
LRKFTEYQIS VSPYNRAGEG KMSQVRDKTL EDKPGPVGIL RFSDVLMDSV KVSWDEPSQP
NGNVIGYIVN YKGYRMQEEF KNEDQQRTSR NYFDTHGLAE GVTYFFSVWA ETSAGKGEQR
SANVTIGPSK DGPPPPSKPQ ITSGQSYVTL NWNDVADSDE IVGHLLQAKR VSVAEEAPAN
GYVSQRPRRN EIKGAKSAAQ TAAATSTRPT HPIGEWITLR PTEGRSEKEQ VSYRELQPSS
YYAFRVFTRN VRGIGMASVE TEQLFVPESI PDDPFYTTWW FMALVAMGAF VLIVIIIAIL
CVTGSSAKYR REKRSRSIDS LQLADGNFAS FQLKGTSAAN MTRSRELPTR PGTTQSWVSD
QSREPPAYGS VLGGSRNSGG VMNMYGLATD VIPPLPNSGP PHTSVEAMQK LSALVGRDIR
SQNTAYVTPS ARGGSDNGRN EYMPTRSDLY ATRSEYGRVE YRGHIPSSSG GSGAGSQPQG
SPLQQPEVYD SFDEEEDVVD DDTVIRGDRT MTDGVDDIAR HYGSTDQYRD TWRKVRDTDM
VRAPILTGHP SSAAGRSSTT DSTSEGPWAN IPATPNLTTG FSSFV
