ITBL_CAEEL
ID ITBL_CAEEL Reviewed; 423 AA.
AC Q9GYK2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Uncharacterized integrin beta-like protein C05D9.3;
DE Flags: Precursor;
GN ORFNames=C05D9.3;
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-65, 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-65 AND ASN-274, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080359; CCD63144.1; -; Genomic_DNA.
DR RefSeq; NP_508212.3; NM_075811.5.
DR AlphaFoldDB; Q9GYK2; -.
DR SMR; Q9GYK2; -.
DR BioGRID; 47112; 4.
DR IntAct; Q9GYK2; 1.
DR STRING; 6239.C05D9.3; -.
DR iPTMnet; Q9GYK2; -.
DR EPD; Q9GYK2; -.
DR PaxDb; Q9GYK2; -.
DR PeptideAtlas; Q9GYK2; -.
DR EnsemblMetazoa; C05D9.3a.1; C05D9.3a.1; WBGene00015472.
DR GeneID; 182254; -.
DR UCSC; C05D9.3; c. elegans.
DR CTD; 182254; -.
DR WormBase; C05D9.3a; CE35381; WBGene00015472; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_617105_0_0_1; -.
DR InParanoid; Q9GYK2; -.
DR OMA; CKCGQCQ; -.
DR OrthoDB; 938950at2759; -.
DR PhylomeDB; Q9GYK2; -.
DR PRO; PR:Q9GYK2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015472; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q9GYK2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:WormBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR032695; Integrin_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 2.
DR Pfam; PF18372; I-EGF_1; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SUPFAM; SSF69179; SSF69179; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..423
FT /note="Uncharacterized integrin beta-like protein C05D9.3"
FT /id="PRO_0000250560"
FT TOPO_DOM 17..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 215..350
FT /note="Cysteine-rich tandem repeats"
FT REGION 354..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..217
FT /evidence="ECO:0000250"
FT DISULFID 33..43
FT /evidence="ECO:0000250"
FT DISULFID 36..68
FT /evidence="ECO:0000250"
FT DISULFID 46..57
FT /evidence="ECO:0000250"
FT DISULFID 215..219
FT /evidence="ECO:0000250"
FT DISULFID 230..241
FT /evidence="ECO:0000250"
FT DISULFID 238..280
FT /evidence="ECO:0000250"
FT DISULFID 243..252
FT /evidence="ECO:0000250"
FT DISULFID 254..271
FT /evidence="ECO:0000250"
FT DISULFID 286..291
FT /evidence="ECO:0000250"
FT DISULFID 288..319
FT /evidence="ECO:0000250"
FT DISULFID 293..303
FT /evidence="ECO:0000250"
FT DISULFID 305..310
FT /evidence="ECO:0000250"
FT DISULFID 325..330
FT /evidence="ECO:0000250"
FT DISULFID 332..341
FT /evidence="ECO:0000250"
FT DISULFID 343..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 46223 MW; 0690DA1C7E279C77 CRC64;
MKSRIFFITL LTIVAAQESA DQLCSSFDAQ QSCGQCIKAH AECAWCIDPH SSLTNRCQLK
SKFTNETCTP HLVYSPQTAQ VKIQQNLPLE TKQHDGKTIV RQQPQAVSVR LMPSHSATVS
FKYLHQTDPS RRSTEPETME IQTSDVKDTP LQLKFFIVCD GELKETKSCR VQNNQIVEFK
IEVLVNSCSS TGDITLSVGI LRQRTIAGLY VTTICGCECE KHPEINSRLC HQNGHLVCGQ
CVCDQSRGGD KCECPLASHG VSKASELEDK CRFNSSSPVC SASGKCKCGQ CQCNKPTVTG
KFCQCDNDSC PLAVNGKVCS GNGVCDCGVC KCEMGWERDD CSCSTASNNC VDNGTPAPEE
KDKPESVPEE PEATEKPDDM PSDSDLEKEL DESSSAKEEQ TSSSGVVSRV CVLLTFFLLV
LNF
