PAT2_CAEBR
ID PAT2_CAEBR Reviewed; 1224 AA.
AC A8X3A7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Integrin alpha pat-2 {ECO:0000250|UniProtKB:P34446};
DE AltName: Full=Paralyzed arrest at two-fold protein 2;
DE Flags: Precursor;
GN Name=pat-2 {ECO:0000312|EMBL:CAP27117.2}; ORFNames=CBG06891;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP27117.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP27117.2};
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: Required for muscle development probably through the
CC regulation of the actin-myosin cytoskeleton. During the formation of
CC neuromuscular junctions at the larval stage, negatively regulates
CC membrane protrusion from body wall muscles, probably through lamins
CC such as epi-1, lam-2 and unc-52. Required for distal tip cell migration
CC and dorsal pathfinding. Required for egg-laying. May play a role in
CC cell motility and cell-cell interactions.
CC {ECO:0000250|UniProtKB:P34446, ECO:0000250|UniProtKB:P53708}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha pat-2
CC associates with beta pat-3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3UV74}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q3UV74}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000255}.
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DR EMBL; HE601347; CAP27117.2; -; Genomic_DNA.
DR AlphaFoldDB; A8X3A7; -.
DR SMR; A8X3A7; -.
DR STRING; 6238.CBG06891; -.
DR PRIDE; A8X3A7; -.
DR EnsemblMetazoa; CBG06891.1; CBG06891.1; WBGene00029084.
DR WormBase; CBG06891; CBP34898; WBGene00029084; Cbr-pat-2.
DR eggNOG; KOG3637; Eukaryota.
DR HOGENOM; CLU_004111_4_2_1; -.
DR InParanoid; A8X3A7; -.
DR OMA; KPPLYQP; -.
DR OrthoDB; 743479at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IEA:EnsemblMetazoa.
DR GO; GO:0055120; C:striated muscle dense body; IEA:EnsemblMetazoa.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR GO; GO:0040017; P:positive regulation of locomotion; IEA:EnsemblMetazoa.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IEA:EnsemblMetazoa.
DR GO; GO:1903354; P:regulation of distal tip cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR GO; GO:0072327; P:vulval cell fate specification; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Cell adhesion; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1224
FT /note="Integrin alpha pat-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370206"
FT TOPO_DOM 28..1153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1154..1174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1175..1224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 29..96
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 110..173
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 180..235
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 236..292
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 293..347
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 364..423
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 427..490
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 898..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 622..624
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 941..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1002
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
SQ SEQUENCE 1224 AA; 135935 MW; 8F75B2BB878FB360 CRC64;
MREGSFPRRT RLLCLLAAVV LISTVTSFNI DTKNVVLHHM ANNYFGYSLD FYNEQKGMPV
LVVGAPEAET TNPNLSGIRR PGAVYACSVN RPTCREVHVD KMKGNLKKLN GSHLVPIEDK
AYQFFGATVK SNDKHDKLLM CAPKYKYFYS KFEVIEPVGT CFYAENGFEK TEEFSSCKQE
PARHGRHRLG YGQCGFSGAI PGKKNQDRVF LGAPGVWYWQ GAIFSQNTKN QTDRPNTEYG
SKEYDHDMMG YATATGDFDG DGIDDIVAGV PRGNDLHGKL VLYTSKLKMM INLTDEVSTQ
HGQYCGGALA VADVNKDGRD DIIMGCPFYT DYGSVKDAKT QERKPQYDVG KVIVFLQTAP
GVFGKQLAVV GDDQWGRFGH SLAAAGDLNL DGYNDVIVGA PYAGKNKQGA VYVIHGSKDG
VREKPTQKIE ASQIGHGTAR AFGFAVAGGV DVDGNGMPDI AVGAWKSGNA AVLLTKPVVT
VTGATEPESA LINVEEKNCD VDGKLGKQAC RHINTCFKYE GKGDTPNDLE FDLRFNLDDH
SPEPRAYFLQ KDVKSDRSIK VASGSKTRDH PSSIEQRVRL EKGRQKCFRH RFFASSTMKD
KLSPIHWSVN YTYVESKSGK LRGDKLEPAI DTTVPLSFQN KINIANNCGK DDLCVPDLKV
TAVADREKFL LGTQDNTMLI NVTVQNGGED SYETKLYFDV PQGFEYGGIE SVGADGSAPA
CSPTSDEPDS DGKWTFACDL GNPLPANKVV SSVVRVTASS DKPPLAPISI NAHVNSSNDE
EAHTIADNKV TFTIPVDFKN QLSLNGRSNP EQVDFSMTNK TRSDVFDDNE IGPVVSHLYQ
ISNRGPSEID AATLDIFWPS FSTEGGHLLY IITEPVVNPP NKGRCRVKQL QNVNPLNLRI
TNEHVPTEPP VAKTPNEYSR EEDDESYEDE TTTQSQTHHQ TRTEHTQHHQ GPVHVYERDE
DKIRQNTGNW QYVEDKKKKG DYEYIPDDQE YDGDDFEDDD EDFDRAGSKR VKRAPVPKKK
KKEGSRSGEP RSDKARFSDL REAVKLSKEA GGVVDYKGPL SRASVDCNGL RCTHIECDIY
DLKEDEFVLV EIFSRLYTNT LVDERNPGGD ISSLALARVT STKYNWPHKP TLITAVSTNM
NAIASEEGRD LPWWLYLLAI LIGLAILILL ILLLWRCGFF KRNRPPTEHA ELRAEKQPAA
HYADTQSRYA PQDQYSQGRH GQML
