ID A0A2K6C0H7_MACNE Unreviewed; 746 AA.
AC A0A2K6C0H7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB6 {ECO:0000313|Ensembl:ENSMNEP00000017161.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000017161.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000017161.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}. 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; A0A2K6C0H7; -.
DR Ensembl; ENSMNET00000041386.1; ENSMNEP00000017161.1; ENSMNEG00000032476.1.
DR GeneTree; ENSGT01100000263555; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032476; Expressed in lung and 4 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0008305; C:integrin complex; IEA:UniProt.
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; 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:SF11; INTEGRIN BETA-6; 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; 2.
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 junction {ECO:0000256|ARBA:ARBA00022949};
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
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 668..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..412
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 582..665
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 689..735
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 155..162
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 210..251
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 384..628
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 410..414
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 425..437
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 434..469
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 439..448
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 475..480
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 477..510
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 482..495
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 497..502
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 516..521
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 518..549
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 523..532
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 534..541
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 555..560
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 557..603
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 562..572
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 575..578
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 582..591
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 588..660
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 607..636
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 746 AA; 81556 MW; A5BD724737D9E900 CRC64;
MITYKNFTRP SGVGERCDTP ANLLAKGCQL NFIENPVSQV EILKNKPLSV GRQKNSSDIV
QIAPQSLILK LRPGGAQTLQ VHVRQTEDYP VDLYYLMDLS ASMDDDLNTI KELGSRLSKE
MSKLTSNFRL GFGSFVEKPL SPFVKTTPEE IANPCSSIPY FCLPTFGFKH ILPLTNDAER
FNEIVKNQKI SANIDTPEGG FDAIMQAAVC KEKIGWRNDS LHLLVFVSDA DSHFGMDSKL
AGIVIPNDGL CHLDSKNEYS MSTVLEYPTI GQLIDKLVQN NVLLIFAVTQ EQVHLYENYA
KLIPGATVGL LQKDSGNILQ LIISAYEELR SEVELEVLGD TEGLNLSFTA ICNNGTFFQH
QKKCSHMKVG DTASFNVTVN IPNCERRSRH IIIKPVGLGD ALELLVSPEC NCDCQKEVEV
NSSKCHHGNG SFQCGVCACH PGHMGPRCEC GEDMLSTDSC KEAPDHPSCS GRGDCYCGQC
ICHLSPYGNI YGPYCQCDNF SCVRHKGLLC GDNGDCDCGE CVCRSGWTGE YCNCTTSTDS
CVSEDGVLCS GRGDCVCGKC VCANPGASGP TCERCPTCGD PCNSKRSCIE CHLSAAGQAR
EECVDKCKLA GATISEEEDF SKDGSVSCSL QGENECLITF LITTDNEGKS IIHSISEKDC
PKPPNIPMIM LGVSLAILLI GVVLLCIWKL LVSFHDRKEV AKFEAERSKA KWQTGTNPLY
RGSTSTFKNV TYKHREKQKV DLSTDG
//
