ID A0A455AFF1_PHYMC Unreviewed; 781 AA.
AC A0A455AFF1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB6 {ECO:0000313|RefSeq:XP_028334159.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028334159.1};
RN [1] {ECO:0000313|RefSeq:XP_028334159.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028334159.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_028334159.1; XM_028478358.2.
DR AlphaFoldDB; A0A455AFF1; -.
DR Proteomes; UP000248484; Chromosome 2.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
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; 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:SF11; INTEGRIN BETA-6; 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; 2.
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 junction {ECO:0000256|ARBA:ARBA00022949};
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:UP000248484};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..781
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019741330"
FT TRANSMEM 702..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..71
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 30..454
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 624..699
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 723..759
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 23..454
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 31..41
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 34..70
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 44..59
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 197..204
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 252..293
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 394..406
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 426..662
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 452..456
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 467..479
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 476..511
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 481..490
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 517..522
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 519..552
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 524..537
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 539..544
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 558..563
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 560..591
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 565..574
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 597..602
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 599..645
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 604..614
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 617..620
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 624..633
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 630..694
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 649..670
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 781 AA; 85101 MW; FF14B947CEBE346B CRC64;
MGIELLCLFF LFLGRNDHVQ GGCAMGDAET CEDCLLIGPQ CAWCSQENFT HLSGVGERCD
TPANLLAKGC QLTFIENPVS QVEILINKPL SVGRQKNSSS IVQIAPQNLA LKLRPGSEQT
LQVQVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSLLS KEMSKLTSNF RLGFGSFVEK
PISPFMKTTP EEIANPCSSI PYICLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE
GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE
YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GVLQKDSGNI
LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAVCNTGTPF PHQKKCSHMK VGDTASFNVT
VSIPNCERRS RHIIIKPVGL GDALEILVSP ECSCDCEKEV EVNSSRCSNG NGSFQCGVCA
CHPGHMGPHC ECGEDTLSTD SCKEAPELPA CSGRGDCYCG QCICHLSPYG DIYGPYCQCD
NFSCVRHRGL LCGDNGDCDC GECVCRSGWT GEYCNCTTST EPCISEDGAL CSGRGGCVCG
KCVCTNPGAS GPTCERCPTC GDPCNSKWSC IECYLSADGQ AQEDCVDKCK LADFSKDSSV
SCSLRGENEC LITFLITTDN EGKTIIHSIN EKDCPKPPNI PMIMLGVSLA ILLIGVVLLC
IWKLLVSFHD RKEVAKFETE RSKAKWQTTQ NSVIVVKDSS HAALCCILHT STAMDRRRSR
S
//