ID A0A3Q1AYJ5_AMPOC Unreviewed; 782 AA.
AC A0A3Q1AYJ5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB6 {ECO:0000313|Ensembl:ENSAOCP00000006363.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000006363.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000006363.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1AYJ5; -.
DR STRING; 80972.ENSAOCP00000006363; -.
DR Ensembl; ENSAOCT00000004735.1; ENSAOCP00000006363.1; ENSAOCG00000010002.1.
DR GeneTree; ENSGT01100000263555; -.
DR OMA; WIYTVEG; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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 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: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; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..782
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018776353"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..69
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 28..450
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 620..701
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 725..771
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 21..450
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 29..39
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 32..68
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 42..57
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 193..200
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 248..289
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 390..402
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 422..665
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 448..452
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 463..475
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 472..507
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 477..486
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 488..498
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 513..518
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 515..548
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 520..533
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..540
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 554..559
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 556..587
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 561..570
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 572..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 593..598
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 595..640
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 600..610
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..616
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..696
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 644..673
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 782 AA; 85797 MW; E4FA0632B37DC8C3 CRC64;
MGLLLLSLIL RYWINTVEGS CSAGSAVTCD QCVQLSPDCA WCRQENFTDW FSVTERCDTL
DILLEKGCAR GQLEFPISKG QILQDQLLGK KTLHSNSTQI SPQKMALKLR PGSQVTFQVQ
VQHTEDYPVD IYYLMDLSAS MFDDLEMIKD LGSTLSKEMA NLTSKFRMGF GSFVEKPVLP
FIKITEEELA NPCREVGFTC LPTFGYKHVL SLTSNTDKFN EIITMQHVSA NVDVPECGFD
AVMQAAVCGE KIGWRNDSMR LLVFVSDADS HFGMDSKMAG IVIPNDGQCH LDANNEYSMS
TLQEYPTLGQ LVDKVVENNI LLIFAVTEEQ ERNYRNYANL IPGATVGVLA TDSQNILELI
VTAYKELRSE IELEVLGDTE KLQMSFTTIC PNGTVLPDLK RCSNIKPGET VVFNVSVELP
GCLSGVRHFS LKPVGLQDSL EVELESLCSC DCQQPPEANS SQCAEGQGAF QCGVCVCQPG
FLGAQCECNE ESALLSNCRA NNESELCNGQ GECYCGQCVC HASSFGRIYG SYCECDNYSC
VRFRGELCGG HGVCDCGECR CESGWTGEYC NCSSSTEACT SEDGVLCSGR GKCECGRCVC
SVAGASGDKC EKCPTCGDAC SSARACVECH LQDKDDAELC DQRCSAPKIS INTTADYDKG
PSTPCTLMME NECWVSFHVL QDETGTSAYN PQIYGCPEPP NIPMIILGVS LSVVCIGIIL
LAVWKVLVSV HDRKEVAKFE AERAKAKWQS GTNPLFRSST STFKNVTYKN TEREKIITMD
HY
//
