ID   C99L2_PONAB             Reviewed;         218 AA.
AC   Q5RE35;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=CD99 antigen-like protein 2;
DE   AltName: CD_antigen=CD99;
DE   Flags: Precursor;
GN   Name=CD99L2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR857703; CAH89972.1; -; mRNA.
DR   RefSeq; NP_001124928.1; NM_001131456.1.
DR   AlphaFoldDB; Q5RE35; -.
DR   Ensembl; ENSPPYT00000053080; ENSPPYP00000034441; ENSPPYG00000020817.
DR   GeneID; 100171799; -.
DR   KEGG; pon:100171799; -.
DR   CTD; 83692; -.
DR   GeneTree; ENSGT00940000154344; -.
DR   InParanoid; Q5RE35; -.
DR   OrthoDB; 1559463at2759; -.
DR   Proteomes; UP000001595; Chromosome X.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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   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..218
FT                   /note="CD99 antigen-like protein 2"
FT                   /id="PRO_0000340094"
FT   TOPO_DOM        26..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          72..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  23294 MW;  5CDA2E021AAD8B1F CRC64;
     MVAWRSAFLV CLAFSLATLV QRGSGDFDDF NLKDAVKETS SVKQRWNHVT TTTKRPVTTR
     APANTLGNDF DLADALDDRN DRDDGRRKPI AGGGGFSDKD LEDIVGGGEY KPDKGKGDGR
     YGSNDDPGSG MVAETGTIAG VASALAMALI GAVSSYISYQ QKKFCFSIQH AAEGQEGLNA
     DYVKGENLEA VVCEEPQVKY SALHTQSAEP PPSEPARI