C99L2_BOVIN
ID C99L2_BOVIN Reviewed; 217 AA.
AC A1A4K1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=CD99 antigen-like protein 2;
DE AltName: CD_antigen=CD99;
DE Flags: Precursor;
GN Name=CD99L2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in a late step of leukocyte extravasation
CC helping cells to overcome the endothelial basement membrane. Acts at
CC the same site as, but independently of, PECAM1 (By similarity).
CC Homophilic adhesion molecule, but these interactions may not be
CC required for cell aggregation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell
CC junction {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
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DR EMBL; BC126619; AAI26620.1; -; mRNA.
DR RefSeq; NP_001077227.1; NM_001083758.1.
DR AlphaFoldDB; A1A4K1; -.
DR STRING; 9913.ENSBTAP00000054220; -.
DR PaxDb; A1A4K1; -.
DR PRIDE; A1A4K1; -.
DR Ensembl; ENSBTAT00000070875; ENSBTAP00000069370; ENSBTAG00000052670.
DR GeneID; 613644; -.
DR KEGG; bta:613644; -.
DR CTD; 83692; -.
DR VEuPathDB; HostDB:ENSBTAG00000052670; -.
DR VGNC; VGNC:106678; CD99L2.
DR eggNOG; ENOG502RZ6C; Eukaryota.
DR GeneTree; ENSGT00940000154344; -.
DR HOGENOM; CLU_2378281_0_0_1; -.
DR InParanoid; A1A4K1; -.
DR OMA; EDIAWGG; -.
DR OrthoDB; 1559463at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000052670; Expressed in hypothalamus and 105 other tissues.
DR ExpressionAtlas; A1A4K1; baseline.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl.
DR GO; GO:2000409; P:positive regulation of T cell extravasation; IEA:Ensembl.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 2.
DR Pfam; PF12301; CD99L2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..217
FT /note="CD99 antigen-like protein 2"
FT /id="PRO_0000340091"
FT TOPO_DOM 26..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 36..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 22987 MW; 0B4A59BE1477AA93 CRC64;
MVAWRWACLI CLAFSLTTLV QRGSGDTGGF RLEDAVEGTS SVKQRWDHVT TTTRRPGATR
APAKPAGPPA EDDFNLADAL DDQNDRDHDR KKPSIGGGGF SDKDLEDIVG GGDYKPDKGK
GGGQYGGGDN SDDSGMSAET GTIAGVASAL AMALIGAVSS YISYQQKKFC FSIQQGLNAD
YVKGENLEAV VCEEPQVKYS ALQTQSTEPP PPEPPRI