Q61092
uniprot
Q61092
canonical
amino_acid_sequence
MPALWLSCCLGVALLLPAAQATSRREVCDCNGKSRQCVFDQELHRQTGSGFRCLNCNDNTAGVHCERCREGFYRHRDRDRCLPCNCHSKGSLSAGCDNSGQCRCKPGVTGQRCDRCQPGFHMLTDAGCTRDQGQLDSKCDCDPAGISGPCDSGRCVCKPAVTGERCDRCRPGYYHLDRANPEGCTQCFCYGHSASCHASADFSVHKITSTFSQDVDGWKAVQRNGAPAKLHWSQRHRDVFSSARRSDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRQPSAYDVILEGAGLQIRAPLMAPGKTLPCGITKTYTFRLNEHPSSHWSPQLSYFEYRRLLRNLTALLIRATYGEYSTGYIDNVTLVSARPVSGAPAPWVERCVCPAGYKGQFCQECASGYKRDSARLGPFGACVPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGFFGDPFGERGPVRPCQRCQCNNNVDPNASGNCDQLTGRCLKCIYNTAGVYCDQCKAGYFGDPLAPNPADKCRACNCSPMGSEPGECRGDGSCVCKPGFGGLNCDHAALTSCPACYNQVKIQMDQFTQQLQSLEALVSKAQGGGGGGTVPVQLEGRIEQAEQALQDILGEAQISEGAMRAVAVRLAKARSQENDYKTRLDDLKMTAERIRALGSQHQNRVQDTSRLISQMRLSLAGSEALLENTNIHSSEHYVGPNDFKSLAQEATRKADSHAESANAMKQLARETEDYSKQALSLARKLLSGGGGSGSWDSSVVQGLMGKLEKTKSLSQQLSLEGTQADIEADRSYQHSLRLLDSASQLQGVSDLSFQVEAKRIRQKADSLSNLVTRQTDAFTRVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKNRAQEALSMGNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLSSISQKVADASDKTQQAETALGSATADTQRAKNAAREALEISSEIELEIGSLNLEANVTADGALAMEKGTATLKSEMREMIELARKELEFDTDKDTVQLVITEAQQADARATSAGVTIQDTLNTLDGILHLIDQPGSVDEEGMMLLEQGLFQAKTQINSRLRPLMSDLEERVRRQRNHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ
uniprot
proteins
function
FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
uniprot
proteins
mass_dalton
130161
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="R->A: No change to herarin-binding."; /evidence="ECO:0000269|PubMed:11733994"; MUTAGEN 78; /note="R->A: No change to herarin-binding."; /evidence="ECO:0000269|PubMed:11733994"; MUTAGEN 202; /note="F->A: No fibulin-1C binding. No change to fibulin-2 binding."; /evidence="ECO:0000269|PubMed:11733994"; MUTAGEN 206; /note="K->A: No fibulin-1C binding. No change to fibulin-2 binding."; /evidence="ECO:0000269|PubMed:11733994"; MUTAGEN 442; /note="C->S: 20-fold reduction to fibulin-2 binding."; /evidence="ECO:0000269|PubMed:11733994"; MUTAGEN 445; /note="C->S: 20-fold reduction to fibulin-2 binding."; /evidence="ECO:0000269|PubMed:11733994
uniprot
proteins
post_translational_modification
PTM: O-glycosylated; contains chondroitin sulfate (CS). {ECO:0000250|UniProtKB:Q13753}.
uniprot
proteins
pubmed
11733994
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7882992
uniprot
proteins
sequence_length
1191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
uniprot
proteins