F11
entrez
109821
canonical
uniprot
Q91Y47
canonical
ensembl
ENSMUSG00000031645
resolver
ensp
ENSMUSP00000034064
resolver
enst
ENSMUST00000034064
resolver
genesymbol
F11
resolver
uniprot
Q9DAT3
resolver
uniprot_entry
FA11_MOUSE
resolver
uniprot_sec
Q9DAT3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250|UniProtKB:P03951}.
uniprot
proteins
amino_acid_sequence
MTSLHQVLYFIFFASVSSECVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDPTKWFACILKDSVTEILPMVNMTGAISGYSFKQCPQQLSTCSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPSVDHRKMCLLKYTRTGTPTTITKLNGVVSGFSLKSCGLSNLACIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESQRHLCLLKTSESGLPSTRITKSHALSGFSLQHCRHSVPVFCHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNERNRRGRCYLKLSSNGSPTRILHGRGGISGYSLRLCKMDNVCTTKINPRVVGGAASVHGEWPWQVTLHISQGHLCGGSIIGNQWILTAAHCFSGIETPKKLRVYGGIVNQSEINEGTAFFRVQEMIIHDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRYRRHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKTQTV
uniprot
proteins
ec_number
3.4.21.27
uniprot
proteins
function
FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. {ECO:0000250|UniProtKB:P03951}.
uniprot
proteins
mass_dalton
69789
uniprot
proteins
post_translational_modification
PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-389 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen. Activated by F12 (activated); the presence of negatively charged surfaces accelerates activation (By similarity). Activated by F2 (thrombin); the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate, strongly accelerates activation (By similarity). Autoactivated; the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate, accelerates autoactivation and autolysis (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P03951}.; PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. {ECO:0000250|UniProtKB:P03951}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
protein_family
Plasma kallikrein subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
9242536
uniprot
proteins
sequence_length
624
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins