ID S7MHQ7_MYOBR Unreviewed; 760 AA.
AC S7MHQ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE Flags: Fragment;
GN ORFNames=D623_10031085 {ECO:0000313|EMBL:EPQ02950.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ02950.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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}.
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 EMBL; KE161298; EPQ02950.1; -; Genomic_DNA.
DR AlphaFoldDB; S7MHQ7; -.
DR eggNOG; KOG1226; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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; 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; 3.
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:SF25; INTEGRIN BETA-3; 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.
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|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:UP000052978};
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 691..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..48
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 10..433
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 606..690
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 714..760
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 11..21
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 14..47
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 24..36
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 175..182
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 230..271
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 372..384
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 404..653
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 431..435
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 446..458
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 455..493
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 460..469
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 471..484
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 499..504
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 501..534
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 506..519
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 521..526
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 540..545
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..573
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 547..556
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 558..565
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 579..584
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 581..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 586..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 599..602
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 606..615
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 612..685
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 633..661
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPQ02950.1"
SQ SEQUENCE 760 AA; 84050 MW; 73D54A7AF43B60FB CRC64;
NICTTRGVSS CQQCLAVSPM CAWCSDQTLT PGSPRCNLKE NLLKDNCALE SIEFPLSEVR
ILEARPLSDK GSGDSSQITQ VSPQRIALRL RPDDSKSFSI QVRQVEDYPV DIYYLMDLSY
SMKDDLSSIQ NLGTKLASQM RKLTSNLRIG FGAFVDKPAS PYMYISPPEA LKNPCYDMKA
TCLPMFGYKH VLTLTDQVNR FNEEVKKQSV SRNRDGPEGG FDAIMQATVC DEKIGWRNDA
SHLLVFTTDA KTHIALDGRL AGIVQPNDGQ CHVGSDNHYS ASTTMDYPSL GLMTEKLSQK
NINLIFAVTE GVVKLYQNYS ELIPGTTVGV LSADSSNVLQ LIVDSYGKIR SKVELEVRDL
PEELSLSFNA TCLNNEVIPG LKSCVGLKIG DTVSFSIEAK VRGCPQEKEK SFTIKPVGFK
DSLTVQVTFD CDCACQAHAE PYSRRCNNGN GTFECGVCRC GPGWLGSQCE CSEEDYRPSQ
QDECSPQEGQ PVCSQRGECL CGQCVCHSSD FGKITGKYCE CDDFSCVRYK GEMCSGHGQC
SCGDCLCDSD WTGYYCNCTT RTDTCMSSNG LLCSGRGKCE CGSCVCIQPG SYGTTCEKCP
TCPDACTFKK ECVECKKFDH GTLYTENTCN RYCRDEVESV KELKDTGKDA VNCTYKNEDD
CVIRFQYYED SSGKSILYVV EEPECPKGPD ILVVLLSVMG AILLIGLATL LIWKLLITIH
DRKEFAKFEE ERARAKWDTA NNPLYKEATS TFTNITYRGT
//
