GenomeNet

Database: UniProt
Entry: A0A8D0A3R8_SANLU
LinkDB: A0A8D0A3R8_SANLU
Original site: A0A8D0A3R8_SANLU 
ID   A0A8D0A3R8_SANLU        Unreviewed;       780 AA.
AC   A0A8D0A3R8;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=itgb5 {ECO:0000313|Ensembl:ENSSLUP00000050141.1};
OS   Sander lucioperca (Pike-perch) (Perca lucioperca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Luciopercinae; Sander.
OX   NCBI_TaxID=283035 {ECO:0000313|Ensembl:ENSSLUP00000050141.1, ECO:0000313|Proteomes:UP000694568};
RN   [1] {ECO:0000313|Ensembl:ENSSLUP00000050141.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSLUP00000050141.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) 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   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A8D0A3R8; -.
DR   Ensembl; ENSSLUT00000051631.1; ENSSLUP00000050141.1; ENSSLUG00000020388.1.
DR   GeneTree; ENSGT01150000286919; -.
DR   Proteomes; UP000694568; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR   GO; GO:0008305; C:integrin complex; IEA:TreeGrafter.
DR   GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR   GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0043149; P:stress fiber assembly; IEA:TreeGrafter.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:TreeGrafter.
DR   FunFam; 2.10.25.10:FF:000043; Integrin beta; 1.
DR   FunFam; 2.10.25.10:FF:000075; Integrin beta; 1.
DR   FunFam; 2.10.25.10:FF:000258; Integrin beta; 1.
DR   FunFam; 3.30.1680.10:FF:000002; Integrin beta; 1.
DR   FunFam; 3.40.50.410:FF:000002; Integrin beta; 1.
DR   FunFam; 4.10.1240.30:FF:000001; Integrin beta; 1.
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; EGF_integrin_1.
DR   InterPro; IPR057073; EGF_integrin_2.
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; IPR057243; Integrin_I-EGF_CS.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF26; INTEGRIN BETA-5; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF23105; EGF_integrin; 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; I_EGF_1; 1.
DR   PROSITE; PS52047; I_EGF_2; 3.
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|ARBA:ARBA00023157,
KW   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694568};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        702..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..61
FT                   /note="PSI"
FT                   /evidence="ECO:0000259|SMART:SM00423"
FT   DOMAIN          20..445
FT                   /note="Integrin beta subunit VWA"
FT                   /evidence="ECO:0000259|SMART:SM00187"
FT   DOMAIN          617..701
FT                   /note="Integrin beta subunit tail"
FT                   /evidence="ECO:0000259|SMART:SM01242"
FT   DOMAIN          725..769
FT                   /note="Integrin beta subunit cytoplasmic"
FT                   /evidence="ECO:0000259|SMART:SM01241"
FT   DISULFID        21..31
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        24..60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        34..49
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        245..286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        383..395
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        415..664
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        443..447
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        466..504
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        471..480
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        482..495
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        510..515
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        512..545
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        517..530
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        532..537
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        551..556
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        553..584
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        558..567
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        590..595
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        592..640
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        597..607
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        610..613
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        617..626
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        623..696
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        644..672
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ   SEQUENCE   780 AA;  85590 MW;  C258A0C186242916 CRC64;
     MISSHPFSGL NMCMSGSATS CEECLLIHPS CAWCAQEEFG RGRTLTSRCD LSQNLQKRGC
     EARFIEYPTS SISVLQNMPL SSKGSGLTQY GVVQIMPQKI SLSLRPGDQT WFGLQVRQVE
     DYPVDLYYLM DLSLSMKDDL DTIRNLGTKL ALEMSKLTSN FRLGFGSFVD KNMSPFSYTA
     SKYQENPCNG YKLFPNCVPT FGFRHILSLT DKVDRFNEEV QKQMVSRNRD APEGGFDAIL
     QAAVCKEEIG WRKEAYHLLV FATDDVPHLA LDGRLGGLVQ PHDGQCHLND ENEYSASEKM
     VRRAALSVVL LTNRAVSLTL SLISSLPKDF TALIPGTTVE ILDQDSKNVI QLIIAAYNNI
     RSKVELSVWD HPEDINLSFT ATCQDGKPLP GLRKCADLKI GDTVSFNVSV EARSCPPRGT
     DQSFTIKPVG FKERLEVSVD YQCDCGCSRT AQTNSSICSS IGTYNCGTCH CEPGYLGARC
     ECQEGEASSM YLSACREAEG KQVCSGRGEC SCNQCLCYES EFGKIYGSYC ECDDFSCARH
     KGVLCSGHGE CHCGECKCHA GYIGDNCNCS TETSSCIADD GQMCSGRGNC VCGRCQCTEP
     GAFGDTCEKC PTCPDACGTK RECIECRLFN SGQLADNQTC QRLCKDEIIT VETLKTEEPG
     AVLCLYKTDN DCVMKFTYSE HASGQSVLTA LKEPECGGGP DALMVLLAVV GSILLVGVVL
     LAVWKLVITI HDRREFSRFQ SARSRARYEM VRSIPLFVFG NKTSSFSRLF CRGTAALCAA
//
DBGET integrated database retrieval system