ID L5L8M4_PTEAL Unreviewed; 741 AA.
AC L5L8M4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN ORFNames=PAL_GLEAN10000535 {ECO:0000313|EMBL:ELK19641.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK19641.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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, ruffle {ECO:0000256|ARBA:ARBA00004466}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Recycling endosome
CC {ECO:0000256|ARBA:ARBA00004172}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; KB030236; ELK19641.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L8M4; -.
DR STRING; 9402.L5L8M4; -.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; L5L8M4; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; 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; 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:SF61; 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; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..407
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 583..671
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 695..741
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 16..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..156
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 204..244
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 378..634
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 405..409
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 420..432
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 429..468
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 434..443
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 445..459
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 474..479
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 476..511
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 481..496
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 498..503
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 517..522
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..550
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 524..533
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..542
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 556..561
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 558..604
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 563..573
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 583..592
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 589..666
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..642
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 741 AA; 82001 MW; C746543F5E01A37E CRC64;
MPTSARCDDL EALKKKGCHP DDIENPRGSK DIKKNKNVTN RSKGTAEKLQ PEDITQIQPQ
QLVLQLRSGE PQTFALKFKR AEDYPIDLYY LMDLSYSMKD DLENVKSLGT DLMNEMRRIT
SDFRIGFGSF VEKTVMPYIS TTPAKLRNPC TSEQNCTSPF SYKNVLSLTD KGEVFNELVG
KQRISGNLDS PEGGFDAIMQ VAVCGSLIGW RNVTRLLVFS TDAGFHFAGD GKLGGIVLPN
DGQCHLENDV YTMSHYYDYP SIAHLVQKLS ENNIQTIFAV TEEFQPVYKE LKNLIPKSAV
GTLSANSSNV IQLIIDAYNS LSSEVILENS KLPEGVTINY KSYCKNGVNG TGENGRKCSN
ISIGDEVQFE ISITSNKCPN KNSETIKIKP LGFTEEVEII LQFICECECQ SEGIPGSPKC
HEGNGTFECG ACRCNEGRVG RHCECSTDEV NSEDMDAYCR KENSSEICSN NGECVCGQCV
CRKRDNTNEI YSGKFCECDN FNCDRSNGLI CGGNGVCKCR VCECNPDYTG SACDCSLDTT
SCMATNGQIC NGRGICECGT CKCTDPKFQG PTCEMCQTCL GVCAEHKECV QCRAFNKGEK
KDTCAQECSH FNITKVENRD KLPQPGQVDP LSHCKEKDVD DCWFYFTYSV NGNNEAIVHV
VETPECPTGP DIIPIVAGVV AGIVLIGLAL LLIWKLLMII HDRREFAKFE KEKMNAKWDT
GENPIYKSAV TTVVNPKYEG K
//
