P98105 · LYAM2_RAT
- ProteinE-selectin
- GeneSele
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids549 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 101-109 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: EPNNKQRNE | ||||||
Binding site | 103 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 109 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 113-118 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: EIYIQR | ||||||
Binding site | 126 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 126-128 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: NDE | ||||||
Binding site | 127 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE-selectin
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP98105
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-494 | Extracellular | ||||
Sequence: WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGIRKVNNVWIWVGTQKPLTEEAKNWAPGEPNNKQRNEDCVEIYIQRPKDSGMWNDERCDKKKLALCYTASCTNTSCSGHGECVETINSYTCKCHPGFLGPKCDQVVTCQEQEYPDHGSLNCTHPFGLFSYNSSCSFSCERGYVPSSMETTVRCTSSGEWSAPAPACHVVECKALTQPAHGVRKCSSNPGSYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSCKAVTCDAIPRPQNGSVSCSNSTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVCKASQCEALSAPQRGHMKCLPSASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTCAGVQCSSLDLPGKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTCEAPANPPRP | ||||||
Transmembrane | 495-516 | Helical | ||||
Sequence: LVVALSVAATSLLTLSSLIYVL | ||||||
Topological domain | 517-549 | Cytoplasmic | ||||
Sequence: KRFFWKKAKKFVPASSCQSLQSFENYQGPSYII |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MNASCFLSALTFVLLIGKSIA | ||||||
Chain | PRO_0000017496 | 22-549 | E-selectin | |||
Sequence: WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGIRKVNNVWIWVGTQKPLTEEAKNWAPGEPNNKQRNEDCVEIYIQRPKDSGMWNDERCDKKKLALCYTASCTNTSCSGHGECVETINSYTCKCHPGFLGPKCDQVVTCQEQEYPDHGSLNCTHPFGLFSYNSSCSFSCERGYVPSSMETTVRCTSSGEWSAPAPACHVVECKALTQPAHGVRKCSSNPGSYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSCKAVTCDAIPRPQNGSVSCSNSTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVCKASQCEALSAPQRGHMKCLPSASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTCAGVQCSSLDLPGKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTCEAPANPPRPLVVALSVAATSLLTLSSLIYVLKRFFWKKAKKFVPASSCQSLQSFENYQGPSYII | ||||||
Glycosylation | 25 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 40↔138 | |||||
Sequence: CQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGIRKVNNVWIWVGTQKPLTEEAKNWAPGEPNNKQRNEDCVEIYIQRPKDSGMWNDERCDKKKLALC | ||||||
Glycosylation | 60 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 111↔130 | |||||
Sequence: CVEIYIQRPKDSGMWNDERC | ||||||
Disulfide bond | 143↔154 | |||||
Sequence: CTNTSCSGHGEC | ||||||
Glycosylation | 145 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 148↔163 | |||||
Sequence: CSGHGECVETINSYTC | ||||||
Disulfide bond | 165↔174 | |||||
Sequence: CHPGFLGPKC | ||||||
Disulfide bond | 180↔225 | |||||
Sequence: CQEQEYPDHGSLNCTHPFGLFSYNSSCSFSCERGYVPSSMETTVRC | ||||||
Glycosylation | 192 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 193↔206 | |||||
Sequence: CTHPFGLFSYNSSC | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 210↔238 | |||||
Sequence: CERGYVPSSMETTVRCTSSGEWSAPAPAC | ||||||
Disulfide bond | 243↔287 | |||||
Sequence: CKALTQPAHGVRKCSSNPGSYPWNTTCTFDCEEGYRRVGAQNLQC | ||||||
Disulfide bond | 256↔269 | |||||
Sequence: CSSNPGSYPWNTTC | ||||||
Glycosylation | 266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 273↔300 | |||||
Sequence: CEEGYRRVGAQNLQCTSSGVWDNEKPSC | ||||||
Disulfide bond | 305↔350 | |||||
Sequence: CDAIPRPQNGSVSCSNSTAGALAFKSSCNFTCEHSFTLQGPAQVEC | ||||||
Glycosylation | 313 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 320 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 333 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 336↔363 | |||||
Sequence: CEHSFTLQGPAQVECSAQGQWTPQIPVC | ||||||
Disulfide bond | 368↔413 | |||||
Sequence: CEALSAPQRGHMKCLPSASAPFQSGSSCKFSCDEGFELKGSRRLQC | ||||||
Disulfide bond | 399↔426 | |||||
Sequence: CDEGFELKGSRRLQCGPRGEWDSEKPTC | ||||||
Disulfide bond | 431↔472 | |||||
Sequence: CSSLDLPGKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTC | ||||||
Glycosylation | 441 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 458↔485 | |||||
Sequence: CPEGWTLNGSSILTCGATGRWSAMLPTC | ||||||
Glycosylation | 465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-139 | C-type lectin | ||||
Sequence: WYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSTLRYSPSYYWIGIRKVNNVWIWVGTQKPLTEEAKNWAPGEPNNKQRNEDCVEIYIQRPKDSGMWNDERCDKKKLALCY | ||||||
Domain | 140-175 | EGF-like | ||||
Sequence: TASCTNTSCSGHGECVETINSYTCKCHPGFLGPKCD | ||||||
Domain | 178-240 | Sushi 1 | ||||
Sequence: VTCQEQEYPDHGSLNCTHPFGLFSYNSSCSFSCERGYVPSSMETTVRCTSSGEWSAPAPACHV | ||||||
Domain | 241-302 | Sushi 2 | ||||
Sequence: VECKALTQPAHGVRKCSSNPGSYPWNTTCTFDCEEGYRRVGAQNLQCTSSGVWDNEKPSCKA | ||||||
Domain | 303-365 | Sushi 3 | ||||
Sequence: VTCDAIPRPQNGSVSCSNSTAGALAFKSSCNFTCEHSFTLQGPAQVECSAQGQWTPQIPVCKA | ||||||
Domain | 366-428 | Sushi 4 | ||||
Sequence: SQCEALSAPQRGHMKCLPSASAPFQSGSSCKFSCDEGFELKGSRRLQCGPRGEWDSEKPTCAG | ||||||
Domain | 429-487 | Sushi 5 | ||||
Sequence: VQCSSLDLPGKMNMSCSGPAVFGTVCEFTCPEGWTLNGSSILTCGATGRWSAMLPTCEA |
Sequence similarities
Belongs to the selectin/LECAM family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length549
- Mass (Da)60,080
- Last updated1996-02-01 v1
- Checksum85CEECDB7B0144C8
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AP16 | A0A8I6AP16_RAT | Sele | 545 | ||
A0A8L2R0D5 | A0A8L2R0D5_RAT | Sele | 519 | ||
A0A0H2UHU5 | A0A0H2UHU5_RAT | Sele | 619 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L25527 EMBL· GenBank· DDBJ | AAA41113.1 EMBL· GenBank· DDBJ | mRNA |