"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PS52047"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 36929, 'pathways': 0, 'proteins': 13478, 'proteomes': 1215, 'sets': 0, 'structural_models': {'alphafold': 11372, 'bfvd': 0}, 'structures': 135, 'taxa': 4211}"	"{}"	"[{'text': '<p>Integrins [[cite:PUB00000811]][[cite:PUB00001505]] are a large family of cell surface receptors that mediate cell\nto cell as well as cell to matrix adhesion. Some integrins recognize the R-G-D\nsequence in their extracellular matrix protein ligand.\nStructurally, integrins consist of a dimer of an alpha and a beta chain. Each\nsubunit has a large N-terminal extracellular domain followed by a\ntransmembrane domain and a short C-terminal cytoplasmic region. Some receptors\nshare a common beta chain while having different alpha chains. The sequence of\na number of different beta chains has been determined and are listed below:\n\n - Integrin beta-1, which  associates with alpha-1 to form a laminin receptor,\n   with alpha-2 to form a  collagen receptor, with  alpha-4  to  interact with\n   VCAM-1, with alpha-5 to form a fibronectin receptor, and with alpha-8.\n - Integrin beta-2, which  associates with alpha-L (LFA-1)  to  interact  with\n   ICAM-1, and with alpha-M (MAC-1) or alpha-X  (p150,95) to form the receptor\n   for the iC3b fragment of the third complement component.\n - Integrin beta-3, which associates with alpha-IIB  to  form  a  receptor for\n   fibrinogen,  fibronectin,  vitronectin and VWF, and with alpha-V  to form a\n   vitronectin receptor.\n - Integrin beta-4, which associates with alpha-6.\n - Integrin beta-5, which associates with alpha-V.\n - Integrin beta-6 [[cite:PUB00002561]].\n - Integrin beta-7 [[cite:PUB00002637]].\n - Integrin beta-8, which associates with alpha-V [[cite:PUB00002660]].\n - The Drosophila myospheroid protein, a probable integrin beta chain.\n\nThe C-terminus of the extracellular region of all the integrin beta chains has\nfour cysteine-rich tandem repeats of forty amino acids, which are variants of\nthe EGF-like domain, termed integrin- or I-EGF domains. The\nI-EGF domain is a small globular domain mainly composed by loops with a small\nanti-parallel beta-sheet constituted of two beta-strands (see {PDB:1L3Y}. The\nstructure is stabilized by four disulfide bonds between the first and fifth,\nsecond and fourth, third and sixth, and seventh and eighth Cys residues. Three\ndisulfide bonds are shared with classical EGF-like domains. The disulfide\nunique to I-EGF domains links the N-terminus to the turn between the two beta-\nstrands. Compared to classical EGF-like modules with three disulfide bonds,\nthe I-EGF module is less elongated, with a nosecone-like shape. The anti-\nparallel sheet between the two beta-strands is shortened because four highly\nconserved residues among classical EGF-like modules are deleted in I-EGF\nmodules. I-EGF repeats in the integrin beta subunit stalk region relay\nactivation signals to the ligand-binding headpiece [[cite:PUB00002660]][[cite:PUB00026914]].\n\nWe have developed a pattern from a section of the I-EGF domain that includes\nfive of the conserved cysteines. We also developed a profile which covers the\nentire I-EGF domain.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	""	False	False	False	"{'PUB00002561': {'PMID': 2365683, 'ISBN': None, 'volume': '265', 'issue': '20', 'year': 1990, 'title': 'Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction.', 'URL': None, 'raw_pages': '11502-7', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Sheppard D', 'Rozzo C', 'Starr L', 'Quaranta V', 'Erle DJ', 'Pytela R.'], 'DOI_URL': 'http://intl.jbc.org/cgi/content/abstract/265/20/11502'}, 'PUB00002660': {'PMID': 1918072, 'ISBN': None, 'volume': '266', 'issue': '29', 'year': 1991, 'title': 'Cloning and expression of a divergent integrin subunit beta 8.', 'URL': None, 'raw_pages': '19650-8', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Moyle M', 'Napier MA', 'McLean JW.'], 'DOI_URL': 'http://intl.jbc.org/cgi/reprint/266/29/19650.pdf'}, 'PUB00026914': {'PMID': 11896403, 'ISBN': None, 'volume': '9', 'issue': '4', 'year': 2002, 'title': 'Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation.', 'URL': None, 'raw_pages': '282-7', 'medline_journal': 'Nat Struct Biol', 'ISO_journal': 'Nat. Struct. Biol.', 'authors': ['Beglova N', 'Blacklow SC', 'Takagi J', 'Springer TA.'], 'DOI_URL': 'http://dx.doi.org/10.1038/nsb779'}, 'PUB00000811': {'PMID': 3028640, 'ISBN': None, 'volume': '48', 'issue': '4', 'year': 1987, 'title': 'Integrins: a family of cell surface receptors.', 'URL': None, 'raw_pages': '549-54', 'medline_journal': 'Cell', 'ISO_journal': 'Cell', 'authors': ['Hynes RO.'], 'DOI_URL': 'http://dx.doi.org/10.1016/0092-8674(87)90233-9'}, 'PUB00002637': {'PMID': 2040616, 'ISBN': None, 'volume': '266', 'issue': '17', 'year': 1991, 'title': 'Complete amino acid sequence of an integrin beta subunit (beta 7) identified in leukocytes.', 'URL': None, 'raw_pages': '11009-16', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Erle DJ', 'Ruegg C', 'Sheppard D', 'Pytela R.'], 'DOI_URL': 'http://intl.jbc.org/cgi/reprint/266/17/11009.pdf'}, 'PUB00001505': {'PMID': 2199285, 'ISBN': None, 'volume': '4', 'issue': '11', 'year': 1990, 'title': 'Integrins and other cell adhesion molecules.', 'URL': None, 'raw_pages': '2868-80', 'medline_journal': 'FASEB J', 'ISO_journal': 'FASEB J.', 'authors': ['Albelda SM', 'Buck CA.'], 'DOI_URL': 'http://www.fasebj.org/cgi/content/abstract/4/11/2868'}}"	""	"{'name': 'Integrins beta chain EGF (I-EGF) domain profile', 'short': 'I_EGF_2'}"	""	""	""	"profile"	"domain"	""