INA1_CAEEL
ID INA1_CAEEL Reviewed; 1139 AA.
AC Q03600;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Integrin alpha ina-1;
DE Flags: Precursor;
GN Name=ina-1; ORFNames=F54G8.3;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH PAT-3.
RX PubMed=9247263; DOI=10.1016/s0896-6273(00)80347-5;
RA Baum P.D., Garriga G.;
RT "Neuronal migrations and axon fasciculation are disrupted in ina-1 integrin
RT mutants.";
RL Neuron 19:51-62(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-788, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-580; ASN-788; ASN-851
RP AND ASN-1026, AND 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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19023419; DOI=10.1371/journal.pgen.1000269;
RA Lucanic M., Cheng H.J.;
RT "A RAC/CDC-42-independent GIT/PIX/PAK signaling pathway mediates cell
RT migration in C. elegans.";
RL PLoS Genet. 4:E1000269-E1000269(2008).
RN [7]
RP FUNCTION, INTERACTION WITH SRC-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20226672; DOI=10.1016/j.cub.2010.01.062;
RA Hsu T.Y., Wu Y.C.;
RT "Engulfment of apoptotic cells in C. elegans is mediated by integrin
RT alpha/SRC signaling.";
RL Curr. Biol. 20:477-486(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22732572; DOI=10.1016/j.ydbio.2012.06.011;
RA Martynovsky M., Wong M.C., Byrd D.T., Kimble J., Schwarzbauer J.E.;
RT "mig-38, a novel gene that regulates distal tip cell turning during
RT gonadogenesis in C. elegans hermaphrodites.";
RL Dev. Biol. 368:404-414(2012).
RN [9]
RP FUNCTION.
RX PubMed=25373777; DOI=10.1016/j.devcel.2014.08.008;
RA Mentink R.A., Middelkoop T.C., Rella L., Ji N., Tang C.Y., Betist M.C.,
RA van Oudenaarden A., Korswagen H.C.;
RT "Cell intrinsic modulation of Wnt signaling controls neuroblast migration
RT in C. elegans.";
RL Dev. Cell 31:188-201(2014).
RN [10]
RP FUNCTION.
RX PubMed=25982859; DOI=10.1016/j.gene.2015.05.030;
RA Meighan C.M., Kann A.P., Egress E.R.;
RT "Transcription factor hlh-2/E/Daughterless drives expression of alpha
RT integrin ina-1 during DTC migration in C. elegans.";
RL Gene 568:220-226(2015).
CC -!- FUNCTION: Plays a role in cell migration, axon fasciculation, and
CC morphogenesis (PubMed:9247263). During gonad morphogenesis, involved in
CC distal tip cell (DTC)-mediated guidance of gonad elongation, in
CC maintaining their sharp tapering morphology and in their migration
CC (PubMed:19023419, PubMed:22732572, PubMed:25982859). Involved in the
CC anterior-posterior positioning of QR neuroblast descendants by
CC regulating the migratory speed of QR.p (PubMed:25373777). Probably by
CC acting as a receptor for apoptotic cells, plays a role in the clearance
CC of apoptotic cells during mid-embryogenesis (PubMed:20226672).
CC {ECO:0000269|PubMed:19023419, ECO:0000269|PubMed:20226672,
CC ECO:0000269|PubMed:22732572, ECO:0000269|PubMed:25373777,
CC ECO:0000269|PubMed:9247263}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha ina-1
CC associates with beta pat-3 (PubMed:9247263). Interacts (via cytoplasmic
CC domain) with src-1 (when phosphorylated at 'Tyr-416')
CC (PubMed:20226672). {ECO:0000269|PubMed:20226672,
CC ECO:0000269|PubMed:9247263}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20226672}; Single-
CC pass type I membrane protein {ECO:0000250}. Cell projection, phagocytic
CC cup {ECO:0000269|PubMed:20226672}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000269|PubMed:20226672}. Note=Enriched at the cell
CC contact with apoptotic cells and in phagocytic pseudopods during
CC apoptotic cell engulfment. Co-localizes with src-1 during phagosome cup
CC formation. {ECO:0000269|PubMed:20226672}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in distal tip cell (DTC)
CC causes DTC morphological and guidance defects such as precocious dorsal
CC turns, a failure to reach the vulva and a bloated distal gonad
CC (PubMed:19023419). Embryos at the comma, 1.5-fold and 2-fold stages
CC have increased number of cell corpses due to a defect in cell
CC engulfment (PubMed:20226672). RNAi-mediated knockdown with mig-38
CC results in enhanced gonad DTC migration (PubMed:22732572).
CC {ECO:0000269|PubMed:19023419, ECO:0000269|PubMed:20226672,
CC ECO:0000269|PubMed:22732572}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; Z19155; CAA79561.1; -; Genomic_DNA.
DR PIR; S28277; S28277.
DR RefSeq; NP_499032.1; NM_066631.4.
DR AlphaFoldDB; Q03600; -.
DR SMR; Q03600; -.
DR BioGRID; 41495; 3.
DR STRING; 6239.F54G8.3; -.
DR iPTMnet; Q03600; -.
DR EPD; Q03600; -.
DR PaxDb; Q03600; -.
DR PeptideAtlas; Q03600; -.
DR PRIDE; Q03600; -.
DR EnsemblMetazoa; F54G8.3.1; F54G8.3.1; WBGene00002081.
DR GeneID; 176296; -.
DR KEGG; cel:CELE_F54G8.3; -.
DR UCSC; F54G8.3; c. elegans.
DR CTD; 176296; -.
DR WormBase; F54G8.3; CE00205; WBGene00002081; ina-1.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000167229; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; Q03600; -.
DR OMA; SGATRYG; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; Q03600; -.
DR Reactome; R-CEL-210991; Basigin interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR Reactome; R-CEL-446107; Type I hemidesmosome assembly.
DR PRO; PR:Q03600; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002081; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IPI:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:WormBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; ISS:WormBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:WormBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:WormBase.
DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IMP:WormBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 1.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 4.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell projection; Cytoplasmic vesicle; Glycoprotein;
KW Integrin; Membrane; Neurogenesis; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1139
FT /note="Integrin alpha ina-1"
FT /id="PRO_0000016331"
FT TOPO_DOM 20..1084
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1085..1106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1107..1139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 21..85
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 111..171
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 180..231
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 242..302
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 307..370
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 378..438
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 448..510
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 1139 AA; 127767 MW; C9AE2C6B97493B8E CRC64;
MRECIISWTL LLCLSCVKSF NLDVNAPIYR YGPSGTNFGY SVAEHFKGDK PVMLIGAPRG
ESGQTGTERA GAMYACDINT FYNGGSNHWC EQVRFEYENV EDYAKRPNET RGRTVHPLGK
NDQLLASTIV SKGTKNGSAL VCAPLIRYHQ TAAYPQGACY ELESNLRLQS TYATCAQKNL
PTTDRHNEYG GCMEGFSAAI TQDTIVTGLI GAVKWTGGVF AKKSSANIFD SVVEKYTMNQ
PNGDMIRTRL VAHDYLGYSV DIGRFGFWYE DGKPITVVSG ATRYGEHGAV IFLPFIQDSS
SKLTLNEDKF IINGTAMGSA FGYSIEVVDL NGDGFDDLIV GAPFEHRSGI DGNFGGIVYV
YFSQGVQRKQ HESHLVFHPP KILKNPDFYS QFGLSITKLG NVDGDKSKLN DFAVGAPFAF
DGAGAVYIYL GTKNIEKFRK KPAQVIKGND LPNLPPGGMR SFGFSLSGGS DMDENGYPDL
LIGSPSKNFV ALLRSRPVIS IETKHKMEKR MVDIDKGVNC PRGAKTCFPL DMVIYVDEET
KRGAELVDFS SDVFMCNLEA IPFRADTTAR GFIEGSHSHN YSWPCGSNSH VQKRTYRQLI
YLPVQESKDW ITPLKFRFTV SIRNEKKPVQ PPQGSQLVDL KHYPVLNKYG ASYEFDVPFN
TLCGEDHTCQ TDLSLKAAFK DIPLTSNGYV SNVGEKDYLD LTFTVENKKE KAYQANFYLE
YNEEELELPQ VQGSKRMIAE TIGKNIVHLP LGNPMNGASK HQFTIQFKLT RGRTEGIGKA
LKFMAHVNST SQETEEELKD NKWEAEVQII KKAELEIYGI SDPDRVFFGG KARAESELEL
EEDIGTMVRH NYTIINHGPW TVRNVEAHIS WPYQLRSRFG RGKNALYLLD VPTITTEFTD
GTSEVRKCFI KQQYEYVNPA EIKLNTKYST QETAPHRVEH RMKREIDEDE EEQSDDLGAV
EENIPWFSTA NFWNLFAIKG GDGRPREVKH LSCQDNTANC FTVICHFDFI DANSAVVIDL
RARLWNATFI EDYSDVESVK IRSFGKLQLD ESQGIDDDPN NNAAFVETSA DPDRPTIGDS
RPIPWWIYVI AAVIGVLILS LIIICLSKCG FFKRNRLDQP SLYTAQLKHE REEWADTGL
