ID A0A0V0TWR6_9BILA Unreviewed; 832 AA.
AC A0A0V0TWR6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=pat-3 {ECO:0000313|EMBL:KRX43358.1};
GN ORFNames=T05_13418 {ECO:0000313|EMBL:KRX43358.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX43358.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX43358.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX43358.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX43358.1}.
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DR EMBL; JYDJ01000121; KRX43358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TWR6; -.
DR STRING; 144512.A0A0V0TWR6; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082:SF62; INTEGRIN BETA PAT-3; 1.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 2.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..832
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006869686"
FT TRANSMEM 757..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..487
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 672..756
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 780..826
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 38..48
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 41..76
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 51..65
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 204..207
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 255..296
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 485..489
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 512..553
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 517..526
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 528..542
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..564
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 561..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 566..581
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 583..588
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 604..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 609..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..627
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 641..646
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 643..694
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 648..662
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..668
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 672..681
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 678..751
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 832 AA; 93800 MW; 7D8B2B79A7AE4B9C CRC64;
MALWLAFVLF TVREVFAQSS SSSSSFPCHA LSGENYTCEH CISQHPSCTW CTMPGFDENN
RHSRCDTSER LLYNGCHDEF IENPKTEYYI ARDEPLSNAG ETEEESEAIQ LKPQEILISM
RPKDVVSFDV TFRQALDYPV DLYYLMDLSF SMADDKQKLT ELGDLLSERM RKITKNFRLG
FGSYVDKKVM PFVDARPERA SRPCETCVDP YGFKNHMSLT KDTRRFAKEV NESAVSGNLD
APEGGFDAIM QALTCTDKIG WREKSRKMIV FSTDAGFHYA GDGRLGGLVV PNDGNCHLDN
DGYYSVSTEF DYPSISQVYQ KIRETQANMI FAVTEEQVPL YQRLRGALPE ISASVGKLAN
DSSNVVELVQ EQYDVCKKMN IINNNFQPRN HHHRCVMCCR KFHKKLSWST TSTLRRVFKF
PTLQHAKGRK VMNRTNVCDG IKVGDTITFN LTLEVTQCTD QREFLIKIGP SGLSEVLLIR
LNVLCDCDCS SKQLDSLSRA AEYCNYNGDL VCGVCQCHHN RVGRRCECEA PGMSTAALDM
MCRKNNDTRA PICEGRGDCD CGRCVCYKRE NINEVYSGQF CECDNFNCPR HKKKLCAGHG
ECVCQQCKCD PGWVGRACEC PISQDSCIAS NGKICNGRGV CECGVCKCFT DPEGIRYSGP
TCEICPTCPT KCIEYKPCVM CQQFKTGPYN ESMCAQCPFT VIPVDELPES NNTGVKCQFV
DQADDCTFYF MYELDEDTNN VTVWVRKEKD CPPPVPVLAI VLGVIAGIVL IGLILLLIWK
LLTIIHDRRE YAKFEKERLM AKWDTGENPI FHPATTTFKN PAYGGNKLSN DL
//
