SDK_CAEBR
ID SDK_CAEBR Reviewed; 2322 AA.
AC Q60ZN5; A8XRF7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein sidekick homolog;
DE AltName: Full=Neuronal IgCAM protein 4;
DE Flags: Precursor;
GN Name=rig-4; ORFNames=CBG17724;
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: 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; HE600976; CAP35231.1; -; Genomic_DNA.
DR RefSeq; XP_002634371.1; XM_002634325.1.
DR AlphaFoldDB; Q60ZN5; -.
DR SMR; Q60ZN5; -.
DR STRING; 6238.CBG17724; -.
DR PRIDE; Q60ZN5; -.
DR EnsemblMetazoa; CBG17724.1; CBG17724.1; WBGene00037279.
DR GeneID; 8576366; -.
DR KEGG; cbr:CBG_17724; -.
DR CTD; 8576366; -.
DR WormBase; CBG17724; CBP18995; WBGene00037279; Cbr-rig-4.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_001875_1_0_1; -.
DR InParanoid; Q60ZN5; -.
DR OMA; EWVVPHK; -.
DR OrthoDB; 134749at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
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; 10.
DR Pfam; PF07679; I-set; 1.
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; 13.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 3: Inferred from homology;
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..2322
FT /note="Protein sidekick homolog"
FT /id="PRO_0000226981"
FT TOPO_DOM 27..2020
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2021..2041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2042..2322
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 450..545
FT /note="Ig-like C2-type 4"
FT DOMAIN 548..639
FT /note="Ig-like C2-type 5"
FT DOMAIN 646..752
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 757..854
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 859..958
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 962..1056
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1060..1155
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1160..1255
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1260..1360
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1364..1458
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1464..1567
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1572..1672
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1674..1774
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1777..1873
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1908..2010
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 732..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2167..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2276..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2207..2225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2279..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1615
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 1864
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 481..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 569..623
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2322 AA; 258961 MW; 3768F30FC1684498 CRC64;
MNYRIFLLFC TTTVLWSVVS TQLVLGKPPI FQNTGPVEQK VAVEGEIVRL KCDDAELAEQ
YEWRVGDASG DLIAASRFAQ VTVSRTNDNQ KYRCVARNTV GAAISPPSVV RSKYLDDFDA
SDESAQYDVL AGIGRHFVLR TPRLLSSRNL DISYSWIKDD SNQVTPDATH FVTANGDLVV
TSVKRDDFGT YKLMASSDDL KEIVSKEYIV KDNGMAPSLQ NTLSIIYFSP ERTIVESSMP
HDEKFDCVTS FEAKDDVRIR WFLNGQPITG SEVGIKTTMN NRRLIISNPS GFTRGEHKLE
CRADAAMGRT SDQNSAYLTF ISRPVLKDLP NEIHKKVGSS LTLKCGVKKK SSMDIKWYRN
GLMMNTQRGK LTIDRIRQED FGLYQCEAVN EAGADMSSVW VKEGDINNDT MVMGMSEDGR
SLEEEISMET PPPRKLKFFD SSKSQEQLFP FTSDIESSQR LTKTPKDLTA ASGTDKITLE
CAAAGSPPPH IVWFLNGNGI QTDSVKYDFS NGDLTIHDIR KSDEGEYTCE ISGTDVKASA
NVQVNGDSLI EYGPADQKSL IGTNVEFSCE VAKEYARKAT VEWYLNDALL PVNGNSGLRI
SRNRKGSLII RQVGPDNTGE YRCRVTVDGR EENASAMLQI IEKPAMPERV RAELHNETMP
AKVRVRWNEG FDGNEPIIKH AIEIRTMGPT GLWSDWTTAI DNIPKDDGKP CCWADIEDLR
PSSTAEFRVV ASNKHGPGKP SLPSSSVTMP QQPPSAAPRN VAASARSPHS VMVQWQQPKE
EQDSGDFLGY VVRYRLAGYS SLTWNEKNLT TKDARNTLVD ELITWREYEI QVAAYNKRGL
GVFSESIEVT TAEGRPTQAP KNVRVKVLNS TAVSLEFTAP EQQRIPGVNL GYKVQFWKGE
PEKGELYKQV ILDPDRRQLS TVVNELEKFG HYNLTVLCFT TPGDGPKSNI LRVVTEEDTP
EAVDELSIAE VMYNGAVLTW NPPMKENGIV TKYTIRHWAS SSPDVKTKHE VDGSTTNITI
DGLQPSTRYG VDVMASTKKG DGPVEETKFE SGVPPELPGR PSMLSIGDIS ATTVQLHFTP
GFDGHTAIRQ WIVEGKMADS SVFAHIFNVS SPKARSIIVT GLRPFTQYQL RLIAENVKGR
GAPSEPSRTF ETLQTNPETP SQRLFTEPVS ATSISVSWTP LLATHWNGQP KGYLIVYREV
DEDNWKEVRT PALRSSEHTV TDLRPFTTYE VNVFSENVFG RSLPTDAVKA RTYESVPSGS
PRNIVVTAEG SKSAIVKWDP VAELSTNGDV IGYKLRVVPE RESLMADETR EIDVPGQSTL
MTKVSNLRPF TSYYVYMSAY TIVGNGPENS TPLSFETLED VPAPPESFQC SQISEQDVRM
KWLPPGSPNG KITNYVISYW KSHEPRSMAI DAQVAGNLLM FSAMSLSPNT QYTFAIKAKN
SKGESEEAVA EVMTSSVRLP VRNAPAPVRD TTSQHLATEI TIRWDESLPR KLTEDAESPV
RAVQVSYQKT NEDEWLTLEK KFEYSKRRAV IKHLSPNSMF RFRIRFIGDF LESSWSPESE
WMRTLPSAPF AQPISLKATP YERNSVQLEW VVPHKSTWNS DAIGYRIHYR EYPSNETWQM
EEIAVHDPHE DREEKVLAKL STFRHYIIRM RLFNSEGEGP FSAPVFVYVG YSIPKRNLTN
IITEPLSSSS IRVKWDAWPK EDSETVTSFK VRYVPVASVL SSVSSEEEVM IVDTNECILS
DLRKFAEYQI SVSPYNRAGE GKMSQVREKT LEDKPGPVGV LRFSDVLMDS VKVSWDEPAQ
PNGMVIGYIV NYKGYRMQEE FKNEDQQRTS RNYFDSHGLA EGVTYFFSVW AETSAGKGEL
RSANVTIGPS KDGPLPPSKP QITSGQSYVT LSWNDVANSD EIVGHLLQAK RVSVAEETEN
GYVSQRPRRN EIRGAKSAAQ TSASSNSNRP THPIGEWITL RPTDGKSEKE QVSYRELQPS
SFYVFRVFTR NVRGIGRASP ETEQLFVPES IPDDPFYTTW WFMALVAMAA FVLIVIIIAI
LCVTGSSAKY RREKRSRSID SLQLADGNFA SFQLKGTSAA NMTRSRELPT RPGTTQSWLS
DQSREPPAYG SVLGDGRNNG GVMNMYGLAT DVIPPLPNSG PPHASLEAMQ KLSALVGRDI
RSQNTAYVVS SSARGSDNER NEYMPTRSDL YGTRSEYGRV EYRGHIPSSS GGSQPQGSPQ
QQQEPYDSFD EEDDVDDDTV IRGDRTMTDG ADDIARHYGS TDQYRDTWRK VRDTDMVRAP
ILTNQQPSSA AGRSSTTDST SEGPWANIPA TPNLTAGFSS FV
