PAT2_CAEEL
ID PAT2_CAEEL Reviewed; 1226 AA.
AC P34446;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Integrin alpha pat-2;
DE AltName: Full=Paralyzed arrest at two-fold protein 2;
DE Flags: Precursor;
GN Name=pat-2 {ECO:0000312|WormBase:F54F2.1};
GN ORFNames=F54F2.1 {ECO:0000312|WormBase:F54F2.1};
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=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 [2]
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-441.
RX PubMed=8106547; DOI=10.1083/jcb.124.4.475;
RA Williams B.D., Waterston R.H.;
RT "Genes critical for muscle development and function in Caenorhabditis
RT elegans identified through lethal mutations.";
RL J. Cell Biol. 124:475-490(1994).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12915588; DOI=10.1242/jcs.00705;
RA Cram E.J., Clark S.G., Schwarzbauer J.E.;
RT "Talin loss-of-function uncovers roles in cell contractility and migration
RT in C. elegans.";
RL J. Cell Sci. 116:3871-3878(2003).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-290; ASN-608
RP AND ASN-819, AND IDENTIFICATION BY MASS 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17606640; DOI=10.1101/gad.1534807;
RA Meighan C.M., Schwarzbauer J.E.;
RT "Control of C. elegans hermaphrodite gonad size and shape by vab-3/Pax6-
RT mediated regulation of integrin receptors.";
RL Genes Dev. 21:1615-1620(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-608; ASN-679
RP AND ASN-819, 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 [9]
RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471;
RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F.,
RA Jacobson L.A., Szewczyk N.J.;
RT "Calpains mediate integrin attachment complex maintenance of adult muscle
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002471-E1002471(2012).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DEP-1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28135265; DOI=10.1371/journal.pgen.1006592;
RA Walser M., Umbricht C.A., Froehli E., Nanni P., Hajnal A.;
RT "beta-Integrin de-phosphorylation by the density-enhanced phosphatase DEP-1
RT attenuates EGFR signaling in C. elegans.";
RL PLoS Genet. 13:E1006592-E1006592(2017).
CC -!- FUNCTION: Required for muscle development probably through the
CC regulation of the actin-myosin cytoskeleton (PubMed:8106547,
CC PubMed:12915588). Component of an integrin containing attachment
CC complex, which is required for muscle maintenance (PubMed:22253611).
CC During the formation of neuromuscular junctions at the larval stage,
CC negatively regulates membrane protrusion from body wall muscles,
CC probably through lamins such as epi-1, lam-2 and unc-52
CC (PubMed:16495308). Required for distal tip cell migration and dorsal
CC pathfinding (PubMed:17606640). Required for egg-laying
CC (PubMed:12915588). May play a role in cell motility and cell-cell
CC interactions (By similarity). Plays a role in vulval development
CC (PubMed:28135265). Probably within the alpha pat-2/beta pat-3 integrin
CC receptor complex, plays a role in the negative regulation of let-23
CC signaling and vulval induction. This is probably partly by restricting
CC the mobility of the let-23 receptor on the plasma membrane of vulval
CC cells which thereby attenuates let-23 signaling (PubMed:28135265).
CC {ECO:0000250|UniProtKB:P53708, ECO:0000269|PubMed:12915588,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17606640,
CC ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:28135265,
CC ECO:0000269|PubMed:8106547}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (Probable).
CC Interacts with beta subunit pat-3 (Probable). Interacts with dep-1
CC (PubMed:28135265). Component of an integrin containing attachment
CC complex, composed of at least pat-2, pat-3, pat-4, pat-6, unc-52, unc-
CC 97 and unc-112 (PubMed:22253611). {ECO:0000269|PubMed:28135265,
CC ECO:0000305, ECO:0000305|PubMed:22253611}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in body-wall muscle cells, distal tip
CC cells, and vulval tissue. {ECO:0000269|PubMed:17606640}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during L3 developmental stage in
CC distal tip cells. {ECO:0000269|PubMed:17606640}.
CC -!- DISRUPTION PHENOTYPE: Severe paralysis at the 1-fold stage of embryonic
CC development followed by an arrest in elongation at 2-fold stage
CC (PubMed:8106547). Loss of myosin and actin organization in embryonic
CC body wall muscles and loss of muscle cell polarization
CC (PubMed:8106547). RNAi-mediated knockdown in post-hatching animals
CC causes paralysis associated with severe disorganization of body wall
CC muscle actin filaments and defects in egg-laying associated with
CC embryonic hatching within the mother (the bag of worms phenotype)
CC (PubMed:12915588). Few surviving adults, are uncoordinated with
CC abnormal body size and shape and have defects in distal tip cells (DTC)
CC migration resulting in abnormal gonad formation (PubMed:17606640).
CC RNAi-mediated knockdown in L4 larval stage, causes ectopic membrane
CC extensions from body wall muscles (PubMed:16495308). RNAi-mediated
CC knockdown results in impaired mobility, mitochondrial fragmentation and
CC disrupted integrin attachment complexes in muscle (PubMed:22253611).
CC This leads to degradation of muscle proteins in the cytosol,
CC myofibrillar defects and disruption of sarcomere organization
CC (PubMed:22253611). RNAi-mediated knockdown in vulval precursor cells in
CC a let-60 gain of function mutant background results in increased vulval
CC induction and an adjacent primary fate (Apf) phenotype whereby
CC secondary vulval precursor cells transform into primary-like vulval
CC cells (PubMed:28135265). {ECO:0000269|PubMed:12915588,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17606640,
CC ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:28135265,
CC ECO:0000269|PubMed:8106547}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; BX284603; CCD71234.1; -; Genomic_DNA.
DR PIR; S44824; S44824.
DR RefSeq; NP_498948.1; NM_066547.3.
DR AlphaFoldDB; P34446; -.
DR SMR; P34446; -.
DR BioGRID; 41442; 5.
DR STRING; 6239.F54F2.1; -.
DR iPTMnet; P34446; -.
DR EPD; P34446; -.
DR PaxDb; P34446; -.
DR PeptideAtlas; P34446; -.
DR EnsemblMetazoa; F54F2.1.1; F54F2.1.1; WBGene00003929.
DR GeneID; 176240; -.
DR KEGG; cel:CELE_F54F2.1; -.
DR UCSC; F54F2.1; c. elegans.
DR CTD; 176240; -.
DR WormBase; F54F2.1; CE00194; WBGene00003929; pat-2.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000169118; -.
DR HOGENOM; CLU_004111_4_2_1; -.
DR InParanoid; P34446; -.
DR OMA; KPPLYQP; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P34446; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-CEL-1566977; Fibronectin matrix formation.
DR Reactome; R-CEL-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:P34446; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003929; Expressed in larva and 3 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; ISS:WormBase.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA: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:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IGI:UniProtKB.
DR GO; GO:0072327; P:vulval cell fate specification; IGI: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; 3.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
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; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1226
FT /note="Integrin alpha pat-2"
FT /id="PRO_0000016332"
FT TOPO_DOM 26..1154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1155..1177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1178..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 27..94
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 108..171
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 178..233
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 234..290
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 291..345
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 362..421
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 425..488
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 709..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 620..622
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 931..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT MUTAGEN 441
FT /note="G->D: In st567; severe paralysis at embryonic 1-fold
FT stage followed by an arrest in elongation at 2-fold stage.
FT Loss of myosin and actin organization in embryonic
FT muscles."
FT /evidence="ECO:0000269|PubMed:8106547"
SQ SEQUENCE 1226 AA; 135940 MW; B9169AD75B88901D CRC64;
MREGSFPRRI GLLLGLLGLL AGVATFNIDT KNVVVHHMAG NYFGYSLDFY HEQKGMPVLV
VGAPEAESNN PNLAGIRRPG AVYACSVNRA TCREVHVDKM KGNLKKLNGS HLVPIEEKSH
QFFGATVRSN DKHDKIVVCA PKYTYFYSKF EVIEPVGTCF YAENGFDNAE EFSSCKQEPA
RHGRHRLGYG QCGFSAAVPG KKNQNRVFIG APGVWYWQGA MFSQNIKNQT DRPNTEYGSK
EYDHDMMGYS TATGDFDGDG IDDIVAGVPR GNDLHGKLVL YTSKLKMMIN LTDEVSTQHG
QYCGGSVAVA DVNKDGRDDI IMGCPFYTDY GSVKDAKTQE RKPQYDVGKV IVMLQTAPGV
FGKQIAVVGD DQWGRFGHAV AAAGDLNLDG YNDVIVGAPY AGKNKQGAVY VIHGSKDGVR
ELPTQKIEGA NIGHGNIKSF GFSLTGNEDV DGNGMPDIAV GAWKSGNAAV LLTKPVVTVT
GQTEPESALI SVEDKNCDVD GKLGKQACKH INTCFKYEGK GDTPNDLEFD LRFNLDDHSP
EPRAYFLQKD VKSDRSIKVA QGSKTRDHPS SIEQRVRLEK GRQKCFRHRF FASSTMKDKL
SPIHWSVNYT YVESKTGKLR GDKLEPAIDT TVPLSFQNKI NIANNCGKDD LCVPDLKVTA
VADREKFLLG TQDNTMLINV TVQNGGEDSY ETKLYFDVPQ GFEYGGIESV GGDGSKSAPA
CSPTSDEPDS DGKWTFACDL GNPLPANKVV SSVVRVTASS DKPPLAPISI NAHVNSSNDE
EAHTVADNKV TFTIPVDFKN QLSLNGRSNP EQVDFSMTNK TRVDAFDDNE IGPVVSHLYQ
ISNRGPSEVD SATLDIFWPS FSTEGGHLLY IITEPVVNPP NKGRCRVKQL QNVNPLNLRI
TNEHVPTEPP VAKTPNEYSR EEDDESYEDE TTTQSQSTRH QSTQHQTHHQ SGPVHVYEKD
EEKIRQNTGN WQYVEDKKKK GDYEYIPDDQ EYDGDDFEEE DDEDFDRAGS KRVKRNPTPK
KKKKGGEHRG EPRSDKARFS DLREAVKLSK EAGGVVDYKG PLSRASVDCN SLRCTHIECD
IYDLKEDEFV LVEIFSRLYT NTLVDEKNPG GDISSLALAR VTSTKYNLPH KPTLITAVST
NMNAIASEEG RDLPWWLYLL AILIGLAILI LLILLLWRCG FFKRNRPPTE HAELRADRQP
NAQYADSQSR YTSQDQYNQG RHGQML
