ID A0A340X9R2_LIPVE Unreviewed; 784 AA.
AC A0A340X9R2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB3 {ECO:0000313|RefSeq:XP_007456802.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007456802.1};
RN [1] {ECO:0000313|RefSeq:XP_007456802.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007456802.1; XM_007456740.1.
DR AlphaFoldDB; A0A340X9R2; -.
DR STRING; 118797.A0A340X9R2; -.
DR GeneID; 103070292; -.
DR KEGG; lve:103070292; -.
DR CTD; 3690; -.
DR InParanoid; A0A340X9R2; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.
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; 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:SF25; INTEGRIN BETA-3; 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 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 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
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:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..784
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016420602"
FT TRANSMEM 715..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..72
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 34..457
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 630..714
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 738..784
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 27..457
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..71
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..60
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 199..206
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 254..295
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 396..408
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 428..677
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 455..459
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 470..482
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 479..517
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 484..493
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 495..508
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 523..528
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 525..558
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 530..543
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 545..550
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 564..569
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 566..597
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 571..580
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 582..589
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 603..608
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 605..653
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 610..620
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 623..626
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 630..639
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 636..709
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 657..685
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 784 AA; 86451 MW; 49F46CC2F0E2624B CRC64;
MRALPLWAAV LVLGALAGVG VGGPNICATR GVSSCQQCLA VSPMCAWCSD EALPPGSPRC
NLKENLLKDD CALESIEFPI SEARILEARP LSDKGSGDSS QITQVSPQRI ALRLRPDDSK
NFSVQVRQVE DYPVDIYYLM DLSYSMKDDL WSIQNLGTKL ASQMRKLTSN LRIGFGAFVD
KPVSPYMYIS PPEALKNPCY DMKTTCLPMF GYKHVLTLTD QVTRFNEEVK KQSVSRNRDA
PEGGFDAIMQ ATVCDEKIGW RNDASHLLVF TTDAKTHIAL DGRLAGIVQP NDGQCHVGSD
NHYAASTTMD YPSLGLMTEK LSQKNINLIF AVTKNVVNLY QNYSELIPGT TVGVLSTDSS
NVLQLIVDAY GKIRSKVELE VRDLPEELSL SFNATCLNNE VIPGLKSCVG LKIGDTVSFS
IEAKVRGCPQ EKEKSFTIKP VGFKDSLTVQ VTFDCDCACQ AQAEPHSHHC NNGNGTFECG
VCRCGPGWLG SQCECSEEDY RPSQQDECSP RVGQPICSQR GECLCGQCVC HSSDFGKIMG
KYCECDDFSC VRYKGEMCSG HGQCSCGDCL CDSDWTGYYC NCTTRTDTCM SSNGLLCSGR
GKCECGSCVC IQPGSYGDTC EKCPTCPDAC TFKKECVECK KFNRGALYEE NSCNRYCRDE
IEPVKELKDT GKDAVNCTYK NEEDCVVRFQ YYEDSSGKSI LYVVEEPECP KGPDILVVLL
SVMGAILLIG LATLLIWKLL ITIHDRKEFA KFEEERARAK WDTANNPLYK EATSTFTNIT
YRGT
//
