ID G3T3B0_LOXAF Unreviewed; 791 AA.
AC G3T3B0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB7 {ECO:0000313|Ensembl:ENSLAFP00000007709.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007709.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007709.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007709.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007709.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007709.3};
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}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {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; G3T3B0; -.
DR STRING; 9785.ENSLAFP00000007709; -.
DR Ensembl; ENSLAFT00000009196.3; ENSLAFP00000007709.3; ENSLAFG00000009194.3.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR InParanoid; G3T3B0; -.
DR OMA; TSCERHR; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0034669; C:integrin alpha4-beta7 complex; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0003366; P:cell-matrix adhesion involved in ameboidal cell migration; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0072678; P:T cell migration; IEA:Ensembl.
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; 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:SF36; INTEGRIN BETA-7; 1.
DR Pfam; PF07974; EGF_2; 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 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:UP000007646};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..791
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003454654"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..92
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 50..476
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 645..721
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 746..791
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 51..61
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 54..91
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 64..80
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 216..223
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 271..311
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 412..428
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 448..688
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 474..478
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 488..500
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 497..537
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 502..511
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 513..527
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 543..548
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 545..574
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 550..559
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 561..566
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 580..585
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 582..613
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 587..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 598..605
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 619..624
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 621..666
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 626..635
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 638..641
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 645..654
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 791 AA; 86333 MW; 94BC14E0E165B375 CRC64;
MVALSMVIWS LLALSRAERE LDTKIPSLGE ATEWGDPDLS LLGSCQPAPS CQQCILSHPS
CAWCKQLNFT ASGEAEERRC AGREELLARG CPLEELEEPR SRQEVLQDYP FSQGARGEGT
VQLAPQRVRV MLRPGEPQRL QVRFLRAEGY PVDLYYLMDL SYSMKDDLEQ VRQLGHDLLL
RLQEVTHSVR IGFGSFVDKT VLPFVSTVPS KLRHPCPTRL EPCQPPFSFH HVLSLTTEAK
VFEQEVGLQN VSGNLDSPEG GFDAILQAAV CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL
GGIFRPSDGR CHLDSNGLYS RSPEFDYPSV GQVAQALSAA NIQPIFAVTS ATLPVYQELS
KLIPKSTVGE LSENSSNVLQ LIMDAYNSLS STVTLQHVSP LPGVHISYES QCGGPKKREG
ETGDRGQCNH VRINQTVNFW VTLQAAHCFT EPQLLRFRAL GFSEELTVEL HTLCDCNCSD
TQPQAAHCSD GQGHLQCGVC SCAPGRRGRL CECSEAELSS PDLESGCRAP NGTGPLCSGK
GRCQCGRCSC SGQSSGRLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG
SVDSCVSSEG GLCSGHGHCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD CAECGAFGTG
PLTTNCSMAC AHANVTLALA PILDDGWCKE RTLDNQLFFF LVEEAGGRVV LRVRPQEKGA
DHTQAIVLGC VGGIVAVGLV LVLAYRISVE IYDRREYSRF EKEQQQLNWN QDNNPLYKSA
ITTTINPRFQ G
//
