ID H2SEI7_TAKRU Unreviewed; 795 AA.
AC H2SEI7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=LOC101067303 {ECO:0000313|Ensembl:ENSTRUP00000010818.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000010818.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000010818.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000010818.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}. Cell
CC projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}.
CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR AlphaFoldDB; H2SEI7; -.
DR Ensembl; ENSTRUT00000010876.3; ENSTRUP00000010818.3; ENSTRUG00000004551.3.
DR GeneTree; ENSGT01090000259987; -.
DR Proteomes; UP000005226; Chromosome 10.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle 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 GO; GO:0007517; P:muscle organ development; 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; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
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; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 725..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..460
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 635..724
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 748..794
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 23..460
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 31..41
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 34..71
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 44..60
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 202..208
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 256..296
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 396..410
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 430..687
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 458..462
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 481..520
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 486..495
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 497..511
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 526..531
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 528..563
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..548
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 550..555
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 569..574
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 571..602
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..585
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 587..594
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..613
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 610..656
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 615..625
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 628..631
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 635..644
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 641..719
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 660..695
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 795 AA; 87584 MW; C7B35094C07E8E48 CRC64;
KNLLPLTPLT FSPFVFNSEG NECIIASAKH CGECIQAGAK CGWCKDPAFL KQGEAVSTRC
DELQSLVKRG CNVDMIESPK GERKILRNKP VTNRKKGGEK LQPHEITQIQ PQKLNLTLRS
GEPQTFDLKF KRAEDYPIDL YYLMDLSYSM KDDLENVKNL GTSLMQKMSK ITSDFQIGFG
SFVEKTVMPY ISTTPAKLLN PCTGDQNCTS PFSYRNVLNL TSDGKQFNTL VGQQQISGNL
DSPEGGFDAI MQVAVCGNLI GWRDVTRLLV FSTDAGFHFA GDGKLGGIVL PNDGKCHLED
NVYTMSHYYD YPSIAHLVQK LSDNNIQTIF AVTEEFQPVY QELKNLIPKS AVGTLSANSS
NVINLIIDAY NSLSSEVILE NSKLPSGVTI TYTSRCKNGV VNGGENGRKC SNISIGDEVT
FSISVTSKGC PNEGMSDTIK IKPLGFTEEL EITLNFICGC DCQKVGINKS PLCHSNGTYE
CGDCRCEDGH VGRECECSSN DVATEDMDRT CRKDNTTDIC SNSGDCVCGT CECKNRDNPE
ERYSGQFCEC DNFSCDRSGN KLCGGHGRCE CRVCVCDLMW AGSACDCSLD NTTCMASNKQ
ICNGRGTCDC GICKCTDPKF QGPTCEICPT CPGVCTEHKE CVQCRTFGTG EKKDTCEKDC
SYFTLIKVKD RDKLPQPNDA AYPVMHCKER DANDCWFYYT YAVNNNTVKE VHVVDSLDCP
AGPDIIPIVA GVVAGIVLIG LALLLIWKLL MIIHDRREFA KFEKEKMNAK WDTGENPIYK
SAVTTVVNPK YEGKC
//
