ID F6PNT9_ORNAN Unreviewed; 819 AA.
AC F6PNT9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSOANP00000009655.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000009655.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000009655.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000009655.3};
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}. Cell
CC projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}.
CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. 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; F6PNT9; -.
DR STRING; 9258.ENSOANP00000009655; -.
DR Ensembl; ENSOANT00000009657.4; ENSOANP00000009655.3; ENSOANG00000006060.5.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000006060; Expressed in ovary and 8 other cell types or tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle 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 GO; GO:0007517; P:muscle organ development; 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; 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:SF28; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 750..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..96
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 54..485
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 661..749
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 773..819
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 55..65
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 58..95
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 68..84
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 227..233
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 281..321
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 455..712
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 483..487
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 498..510
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 507..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 512..521
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 523..537
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 552..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 554..589
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..574
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..581
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 595..600
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 597..628
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..611
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..620
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..639
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 636..682
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 641..651
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 654..657
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 661..670
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 667..744
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 686..720
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 819 AA; 90402 MW; D5A4097607899E20 CRC64;
MGPKLIHCFW RETPIFNKIQ MNLQHIFFVL ASCSICKVFG QTGGNECLKA NAKSCGECIQ
AGPNCGWCTN STFLQEGMPT SARCDDLAAL KSKGCLPEDI ENPRGSKNIR KNKNVTNRSK
GTAEKLQPED ITQIQPQQLV LKLRSGEPQT FALKFKRAED YPIDLYYLMD LSYSMKDDLE
NVKSLGTDLM YEMKRITSDF RIGFGSFVEK TVMPYISTTP AKLRNPCTGD QNCTSPFSYK
NVLNLTDKGE VFNELVGKQH ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA
GFHFAGDGKL GGIVLPNDGR CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE
FQAVYKELKN LIPKSAVGTL SANSSNVIQL IIDAYNSLSS EVILENSKLP EGVTINYKSY
CKNGVNGTGE NGRKCSNISI GDEVQFEISV TANKCPKKGQ NETIKIKPLG FTEEVEINLQ
FICECECQNE GIPESSKCHG GNGTFECGAC RCNEGRVGRH CECSTDEVNS EDMDAYCRKE
NSSEICSNNG ECVCGQCVCR KRDNTNEVYS GKFCECDNFN CDRSNGLICG GNGVCKCRVC
ECNPNFTGSA CDCSLDTSSC LASNGQICNG RGICECGSCK CTDPKFQGPT CEMCQTCLGV
CAEHKECVQC RAFDKGEKKD TCVQECSHFN MTLVENRDKL PQPGQVDPLS HCKEKDADDC
WFYFTYSVNG NNEAIVHVVE TPECPTGPDI IPIVAGVVAG IVLIGLALLL IWKLLMIIHD
RREFAKFEKE KMNAKWDTGE NPIYKSAVTT VVNPKYEGK
//
