ID H2UU50_TAKRU Unreviewed; 802 AA.
AC H2UU50;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=itgb5 {ECO:0000313|Ensembl:ENSTRUP00000040474.2};
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:ENSTRUP00000040474.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000040474.2, 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:ENSTRUP00000040474.2}
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}.
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}.
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DR AlphaFoldDB; H2UU50; -.
DR STRING; 31033.ENSTRUP00000075008; -.
DR Ensembl; ENSTRUT00000040616.3; ENSTRUP00000040474.2; ENSTRUG00000015838.3.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000005226; Chromosome 1.
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; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR040622; I-EGF_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; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF26; INTEGRIN BETA-5; 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 Pfam; PF17205; PSI_integrin; 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 SMART; SM00423; PSI; 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:UP000005226};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..802
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025396533"
FT TRANSMEM 723..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..80
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 39..466
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 638..722
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 746..793
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 40..50
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 43..79
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 53..68
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 205..214
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 262..303
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 404..416
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 436..685
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 464..468
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 487..525
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 503..516
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 531..536
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..566
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 538..551
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 553..558
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 572..577
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..605
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 579..588
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 611..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..661
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 618..628
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 631..634
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 644..717
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..693
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 802 AA; 88649 MW; 36047473E57412C6 CRC64;
AMWIPATWTW RAALTCVLLE TVLRGVRGLN ICTSGSATSC RDCLLIHPSC AWCAQEDFGR
GKTLTSRCDF IQNLQKRGCE PRFVENPSSS ISVLQNIPLS SKGLSQYDVI QIMPQKLALS
LRPGGQTWFE LQVRQVEDYP VDVYYLMDLS LSMKDDLETI RNLGTKLAHE MGKLTSNFRL
GFGTFVDKNM SPFSYTAEKY QENPCSGYKL FPNCVPTFGF RHILPLTDKV DRFNEEVQKQ
MVSRNRDAPE GGFDAILQAA VCKEKIGWRK EAYHLLVFTT DDVPHLALDG RLGGLVEPHD
GQCHLDDNSE YSASTKMDYP SLALLGEKLA ENNIFLIFAV TKQLYIIYKN FTALIPGTTV
EILDQDSKNV IQLIVAAYNN IRSKVELSVW DHPEDISLSF TATCQDGMPL PGFRKCADLK
IGDTVSFNVS VEARSCPPHG ANHSFTIKPV GFKDHLEVSV DYQCDCGCSK TAQVNSSICS
STGTYNCGTC HCEPGYLGAR CECQEGEASS IYLNACREAE GKQVCSGRGE CSCNQCLCYE
SEFGKIYGSF CECDDFSCAR HKGILCSGHG ECHCGECKCH AGYVGDNCNC STETSSCISD
DGRMCSGRGS CACGRCQCTE PGSFGETCEK CPTCPDACAT KRECIECRLF NSGQLTDNQT
CQRLCKDEII TVETLKTDDP GAVLCLYKTD NNCVMKFTYS EHTSGQSVLT TLKEPECSTG
TDALMVLLAV VGSILLVGVV LLAVWKLVIT IHDWREFSRF QSARSRARYE MASNPLYKQP
VSTHDLETDL SMYGKPYNGG MH
//
