ID   ITB5_PAPCY              Reviewed;         655 AA.
AC   Q07441;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Integrin beta-5;
DE   Flags: Fragment;
GN   Name=ITGB5;
OS   Papio cynocephalus (Yellow baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8224922; DOI=10.1016/0378-1119(93)90659-q;
RA   Shoji M., Hayzer D.J., Kim T.M., Runge M.S., Hanson S.R.;
RT   "Human and baboon integrin beta 5 subunit-encoding mRNAs have alternative
RT   polyadenylation sites.";
RL   Gene 133:307-308(1993).
CC   -!- FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for
CC       fibronectin. It recognizes the sequence R-G-D in its ligand.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5 (ITGB5)
CC       associates with alpha-V (ITGAV). Interacts with MYO10. Interacts with
CC       DAB2. Integrin ITGAV:ITGB5 interacts with FBLN5 (via N-terminus) (By
CC       similarity). ITGAV:ITGB5 interacts with CCN3 (By similarity).
CC       {ECO:0000250|UniProtKB:O70309, ECO:0000250|UniProtKB:P18084}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- PTM: The cysteine residues are involved in intrachain disulfide bonds.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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; L12231; AAA16866.1; -; mRNA.
DR   AlphaFoldDB; Q07441; -.
DR   SMR; Q07441; -.
DR   PRIDE; Q07441; -.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027067; Integrin_beta-5.
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; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF26; PTHR10082:SF26; 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   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..655
FT                   /note="Integrin beta-5"
FT                   /id="PRO_0000174222"
FT   TOPO_DOM        <1..575
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        599..655
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..234
FT                   /note="VWFA"
FT   REPEAT          321..368
FT                   /note="I"
FT   REPEAT          369..410
FT                   /note="II"
FT   REPEAT          411..449
FT                   /note="III"
FT   REPEAT          450..486
FT                   /note="IV"
FT   REGION          457..621
FT                   /note="Cysteine-rich tandem repeats"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18084"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   655 AA;  72466 MW;  BAC33A159CBE1596 CRC64;
     DLSLSMKDDL DTIRNLGTKL AEEMRKLTSN FRLGFGSFVD KDISPFSYTA PRYQTNPCIG
     YKLFPNCVPS FGFRHLLPLT DRVDSFNEEV RKQRVSRNRD APEGCFDAVL QAAVCKEKIG
     WRKDALHLLV FTTDDVPHIA LDGKLGGLVQ PHDGQCHLNE ANEYTASNQM DYPSLALLGE
     KLAENNINLI FAVTKNHYML YKNFTALIPG TTVEILDGDS KNIIQLIINA YNSIRSKVEL
     SVWDQPEDLN LFFTATCQDG VSYPGQRKCE GLKIGDTASF EVSVEARSCP SRHTEHVFAL
     QPVGCRDSLE VGVTYNCTCG CSVGLEPNSA RCSGTGTYVC GLCECSPGYL GTRCECQDGE
     NHSVYQNLCR DTEGKPLCSG RGDCSCNQCS CFESEFGKIY GPFCECDNFS CARNKGVLCS
     GHGECHCGEC KCHAGYIGDN CNCSTDISTC RGRDGQICSE RGHCLCGQCQ CTEPGAFGEM
     CEKCPTCPDA CSTKRDCVEC PLLHSGKPDN QTCHSLCRDE VITWVDTIVK DDQEAVLCFY
     KTAKDCVMMF TYVELPSGKS NLTVLREPEC GNTPNAMTIL LAVVGSILLV GLALLAIWKL
     LVTIHDRREF AKFQSERSRA RYEMASNPLY RKPISTHTVD FTFNKFNKSY NGTVD