GenomeNet

Database: UniProt
Entry: F6PPW0_MONDO
LinkDB: F6PPW0_MONDO
Original site: F6PPW0_MONDO 
ID   F6PPW0_MONDO            Unreviewed;       800 AA.
AC   F6PPW0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=ITGB5 {ECO:0000313|Ensembl:ENSMODP00000022896.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000022896.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000022896.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000022896.3}
RP   IDENTIFICATION.
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   RefSeq; XP_007493880.1; XM_007493818.2.
DR   AlphaFoldDB; F6PPW0; -.
DR   STRING; 13616.ENSMODP00000022896; -.
DR   Ensembl; ENSMODT00000023301.4; ENSMODP00000022896.3; ENSMODG00000018360.4.
DR   GeneID; 100020074; -.
DR   KEGG; mdo:100020074; -.
DR   CTD; 3693; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   GeneTree; ENSGT01090000259987; -.
DR   HOGENOM; CLU_011772_0_1_1; -.
DR   InParanoid; F6PPW0; -.
DR   OMA; CVMLFTY; -.
DR   OrthoDB; 5475862at2759; -.
DR   TreeFam; TF105392; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000018360; Expressed in heart and 18 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0034684; C:integrin alphav-beta5 complex; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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:SF26; INTEGRIN BETA-5; 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; 2.
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:UP000002280};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..800
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003344212"
FT   TRANSMEM        721..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..76
FT                   /note="PSI"
FT                   /evidence="ECO:0000259|SMART:SM00423"
FT   DOMAIN          35..463
FT                   /note="Integrin beta subunit VWA"
FT                   /evidence="ECO:0000259|SMART:SM00187"
FT   DOMAIN          635..720
FT                   /note="Integrin beta subunit tail"
FT                   /evidence="ECO:0000259|SMART:SM01242"
FT   DOMAIN          744..791
FT                   /note="Integrin beta subunit cytoplasmic"
FT                   /evidence="ECO:0000259|SMART:SM01241"
FT   DISULFID        36..46
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        39..75
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        49..64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        202..211
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        259..300
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        401..413
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        433..683
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        461..465
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        484..522
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        489..498
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        500..513
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        528..533
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        530..563
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        535..548
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        550..555
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        569..574
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        571..602
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        576..585
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        587..594
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        608..613
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        610..658
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        615..625
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        628..631
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        635..644
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        641..715
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        662..691
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ   SEQUENCE   800 AA;  88568 MW;  A1B3034862EC3A9D CRC64;
     MFRRLWSLSS CFLVFCTLLP QSPGLNICTS GSATSCEECL LINPKCAWCS KEDFGNQRSV
     TSRCDLKANL LKLGCGGELE SPDSSITVLK NLPLSIKGSS PSNADVIQMT PQKISMNLRP
     GDKTPFRVQV RQVEDYPVDL YYLMDLSLSM KDDLDTILNL GTKLAEEMRK LTSNFRLGFG
     SFVDKNISPF SYTAPRYQTN PCIGYKLFPY CVPSFGFRHL LSLTDKVDSF NEEVKKQMVS
     RNKDAPEGGF DAILQAAVCK EKIGWRKEAL HLLVFTSDDV PHIALDGKLG GLVQPHDGQC
     HLNEANEYTA SKQMDYPSLA LLGEKLAENN IHLIFAVTKN HYMLYKNFTA LIPGTTVEIL
     HADSRNIIQL IVNAYNSIRS KVELSVWDNP EDLGLSFTAT CQDGLSYPGQ RKCGDLKIGE
     TVSFEVSVEA RSCPSPDTVH TFTLRPVGFR DALELVVTYN CSCNCASRTE QDSPRCSGNG
     TYTCGTCECH PSYLGSKCEC QEGENRDLYQ NLCREAEGKP LCSGRGECSC NQCSCYESEF
     GKIYGPFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTE TETCLSNDGQ
     ICSGRGYCSC GRCQCIKPGA FGETCEKCPT CPDACSTKRD CVECMLFNSG RLADNQTCQK
     HCRDEVIIQV DSIMKDDQEA VLCFYKTAKD CVMMFTYSEL PSGKSKLMVL KEPECGSAPS
     AMTILLAVVG SILLVGIALL AIWKLLVTIH DRREFAKFQS ERSRARYEMA SNPLYRKPIS
     THTVDFTFNK LNKSYNGTVD
//
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