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Protein

Integrin alpha pat-2

Gene

pat-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for muscle development probably through the regulation of the actin-myosin cytoskeleton (PubMed:8106547, PubMed:12915588). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably through lamins such as epi-1, lam-2 and unc-52 (PubMed:16495308). Required for distal tip cell migration and dorsal pathfinding (PubMed:17606640). Required for egg-laying (PubMed:12915588). May play a role in cell motility and cell-cell interactions (By similarity).By similarity4 Publications

GO - Molecular functioni

  • transmembrane signaling receptor activity Source: WormBase

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • positive regulation of engulfment of apoptotic cell Source: WormBase
  • positive regulation of locomotion Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-CEL-114608. Platelet degranulation.
R-CEL-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-CEL-216083. Integrin cell surface interactions.
R-CEL-3000170. Syndecan interactions.
R-CEL-354192. Integrin alphaIIb beta3 signaling.
R-CEL-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-CEL-372708. p130Cas linkage to MAPK signaling for integrins.
R-CEL-445144. Signal transduction by L1.
SignaLinkiP34446.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha pat-2
Alternative name(s):
Paralyzed arrest at two-fold protein 2
Gene namesi
Name:pat-2
ORF Names:F54F2.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiF54F2.1; CE00194; WBGene00003929; pat-2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 11541129ExtracellularSequence analysisAdd
BLAST
Transmembranei1155 – 117723HelicalSequence analysisAdd
BLAST
Topological domaini1178 – 122649CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: WormBase
  • integrin complex Source: WormBase
  • M band Source: WormBase
  • striated muscle dense body Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Severe paralysis at the 1-fold stage of embryonic development followed by an arrest in elongation at 2-fold stage (PubMed:8106547). Loss of myosin and actin organization in embryonic body wall muscles and loss of muscle cell polarization (PubMed:8106547). RNAi-mediated knockdown in post-hatching animals causes paralysis associated with severe disorganization of body wall muscle actin filaments and defects in egg-laying associated with embryonic hatching within the mother (the bag of worms phenotype) (PubMed:12915588). Few surviving adults, are uncoordinated with abnormal body size and shape and have defects in distal tip cells (DTC) migration resulting in abnormal gonad formation (PubMed:17606640). RNAi-mediated knockdown in L4 larval stage, causes ectopic membrane extensions from body wall muscles (PubMed:16495308).4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi441 – 4411G → D in st567; severe paralysis at embryonic 1-fold stage followed by an arrest in elongation at 2-fold stage. Loss of myosin and actin organization in embryonic muscles. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 12261201Integrin alpha pat-2PRO_0000016332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi108 – 1081N-linked (GlcNAc...)2 Publications
Glycosylationi228 – 2281N-linked (GlcNAc...)2 Publications
Glycosylationi290 – 2901N-linked (GlcNAc...)1 Publication
Glycosylationi608 – 6081N-linked (GlcNAc...)2 Publications
Glycosylationi679 – 6791N-linked (GlcNAc...)1 Publication
Glycosylationi775 – 7751N-linked (GlcNAc...)Sequence analysis
Glycosylationi819 – 8191N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiP34446.
PaxDbiP34446.
PRIDEiP34446.

Expressioni

Tissue specificityi

Expressed in body-wall muscle cells, distal tip cells, and vulval tissue.1 Publication

Developmental stagei

Up-regulated during L3 developmental stage in distal tip cells.1 Publication

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Alpha pat-2 associates with beta pat-3.

Protein-protein interaction databases

BioGridi41442. 2 interactions.
STRINGi6239.F54F2.1.

Structurei

3D structure databases

ProteinModelPortaliP34446.
SMRiP34446. Positions 26-900.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 9468FG-GAP 1Add
BLAST
Repeati108 – 17164FG-GAP 2Add
BLAST
Repeati178 – 23356FG-GAP 3Add
BLAST
Repeati234 – 29057FG-GAP 4Add
BLAST
Repeati291 – 34555FG-GAP 5Add
BLAST
Repeati362 – 42160FG-GAP 6Add
BLAST
Repeati425 – 48864FG-GAP 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi620 – 6223Cell attachment siteSequence analysis

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000115457.
InParanoidiP34446.
OMAiMCIPDLK.
OrthoDBiEOG71ZP14.
PhylomeDBiP34446.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 4 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREGSFPRRI GLLLGLLGLL AGVATFNIDT KNVVVHHMAG NYFGYSLDFY
60 70 80 90 100
HEQKGMPVLV VGAPEAESNN PNLAGIRRPG AVYACSVNRA TCREVHVDKM
110 120 130 140 150
KGNLKKLNGS HLVPIEEKSH QFFGATVRSN DKHDKIVVCA PKYTYFYSKF
160 170 180 190 200
EVIEPVGTCF YAENGFDNAE EFSSCKQEPA RHGRHRLGYG QCGFSAAVPG
210 220 230 240 250
KKNQNRVFIG APGVWYWQGA MFSQNIKNQT DRPNTEYGSK EYDHDMMGYS
260 270 280 290 300
TATGDFDGDG IDDIVAGVPR GNDLHGKLVL YTSKLKMMIN LTDEVSTQHG
310 320 330 340 350
QYCGGSVAVA DVNKDGRDDI IMGCPFYTDY GSVKDAKTQE RKPQYDVGKV
360 370 380 390 400
IVMLQTAPGV FGKQIAVVGD DQWGRFGHAV AAAGDLNLDG YNDVIVGAPY
410 420 430 440 450
AGKNKQGAVY VIHGSKDGVR ELPTQKIEGA NIGHGNIKSF GFSLTGNEDV
460 470 480 490 500
DGNGMPDIAV GAWKSGNAAV LLTKPVVTVT GQTEPESALI SVEDKNCDVD
510 520 530 540 550
GKLGKQACKH INTCFKYEGK GDTPNDLEFD LRFNLDDHSP EPRAYFLQKD
560 570 580 590 600
VKSDRSIKVA QGSKTRDHPS SIEQRVRLEK GRQKCFRHRF FASSTMKDKL
610 620 630 640 650
SPIHWSVNYT YVESKTGKLR GDKLEPAIDT TVPLSFQNKI NIANNCGKDD
660 670 680 690 700
LCVPDLKVTA VADREKFLLG TQDNTMLINV TVQNGGEDSY ETKLYFDVPQ
710 720 730 740 750
GFEYGGIESV GGDGSKSAPA CSPTSDEPDS DGKWTFACDL GNPLPANKVV
760 770 780 790 800
SSVVRVTASS DKPPLAPISI NAHVNSSNDE EAHTVADNKV TFTIPVDFKN
810 820 830 840 850
QLSLNGRSNP EQVDFSMTNK TRVDAFDDNE IGPVVSHLYQ ISNRGPSEVD
860 870 880 890 900
SATLDIFWPS FSTEGGHLLY IITEPVVNPP NKGRCRVKQL QNVNPLNLRI
910 920 930 940 950
TNEHVPTEPP VAKTPNEYSR EEDDESYEDE TTTQSQSTRH QSTQHQTHHQ
960 970 980 990 1000
SGPVHVYEKD EEKIRQNTGN WQYVEDKKKK GDYEYIPDDQ EYDGDDFEEE
1010 1020 1030 1040 1050
DDEDFDRAGS KRVKRNPTPK KKKKGGEHRG EPRSDKARFS DLREAVKLSK
1060 1070 1080 1090 1100
EAGGVVDYKG PLSRASVDCN SLRCTHIECD IYDLKEDEFV LVEIFSRLYT
1110 1120 1130 1140 1150
NTLVDEKNPG GDISSLALAR VTSTKYNLPH KPTLITAVST NMNAIASEEG
1160 1170 1180 1190 1200
RDLPWWLYLL AILIGLAILI LLILLLWRCG FFKRNRPPTE HAELRADRQP
1210 1220
NAQYADSQSR YTSQDQYNQG RHGQML
Length:1,226
Mass (Da):135,940
Last modified:February 1, 1994 - v1
Checksum:iB9169AD75B88901D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081385 Genomic DNA. Translation: CCD71234.1.
PIRiS44824.
RefSeqiNP_498948.1. NM_066547.3.
UniGeneiCel.10427.

Genome annotation databases

EnsemblMetazoaiF54F2.1; F54F2.1; WBGene00003929.
GeneIDi176240.
KEGGicel:CELE_F54F2.1.
UCSCiF54F2.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081385 Genomic DNA. Translation: CCD71234.1.
PIRiS44824.
RefSeqiNP_498948.1. NM_066547.3.
UniGeneiCel.10427.

3D structure databases

ProteinModelPortaliP34446.
SMRiP34446. Positions 26-900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41442. 2 interactions.
STRINGi6239.F54F2.1.

Proteomic databases

EPDiP34446.
PaxDbiP34446.
PRIDEiP34446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF54F2.1; F54F2.1; WBGene00003929.
GeneIDi176240.
KEGGicel:CELE_F54F2.1.
UCSCiF54F2.1. c. elegans.

Organism-specific databases

CTDi176240.
WormBaseiF54F2.1; CE00194; WBGene00003929; pat-2.

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000115457.
InParanoidiP34446.
OMAiMCIPDLK.
OrthoDBiEOG71ZP14.
PhylomeDBiP34446.

Enzyme and pathway databases

ReactomeiR-CEL-114608. Platelet degranulation.
R-CEL-1236973. Cross-presentation of particulate exogenous antigens (phagosomes).
R-CEL-216083. Integrin cell surface interactions.
R-CEL-3000170. Syndecan interactions.
R-CEL-354192. Integrin alphaIIb beta3 signaling.
R-CEL-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-CEL-372708. p130Cas linkage to MAPK signaling for integrins.
R-CEL-445144. Signal transduction by L1.
SignaLinkiP34446.

Miscellaneous databases

NextBioi891720.
PROiP34446.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 4 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations."
    Williams B.D., Waterston R.H.
    J. Cell Biol. 124:475-490(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-441.
  4. "Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans."
    Cram E.J., Clark S.G., Schwarzbauer J.E.
    J. Cell Sci. 116:3871-3878(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-290; ASN-608 AND ASN-819, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "FGF negatively regulates muscle membrane extension in Caenorhabditis elegans."
    Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.
    Development 133:1263-1275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Control of C. elegans hermaphrodite gonad size and shape by vab-3/Pax6-mediated regulation of integrin receptors."
    Meighan C.M., Schwarzbauer J.E.
    Genes Dev. 21:1615-1620(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  8. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108; ASN-228; ASN-608; ASN-679 AND ASN-819, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

Entry informationi

Entry nameiPAT2_CAEEL
AccessioniPrimary (citable) accession number: P34446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 13, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.