C99L2_RAT
ID C99L2_RAT Reviewed; 246 AA.
AC Q8R1R5; Q9JJL7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=CD99 antigen-like protein 2;
DE AltName: Full=MIC2-like protein 1;
DE AltName: Full=Rhombencephalic expression protein 40 kDa;
DE Short=Protein rhombex-40;
DE AltName: CD_antigen=CD99;
DE Flags: Precursor;
GN Name=Cd99l2; Synonyms=Mic2l1, Rhombex40;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=10834302; DOI=10.1016/s0024-3205(00)00545-2;
RA Shimokawa N., Jingu H., Okada J., Miura M.;
RT "Molecular cloning of Rhombex-40 a transmembrane protein from the ventral
RT medullary surface of the rat brain by differential display.";
RL Life Sci. 66:2183-2191(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Lewis; TISSUE=Thymus;
RX PubMed=12706889; DOI=10.1016/s0378-1119(03)00401-3;
RA Suh Y.H., Shin Y.K., Kook M.-C., Oh K.I., Park W.S., Kim S.H., Lee I.-S.,
RA Park H.J., Huh T.-L., Park S.H.;
RT "Cloning, genomic organization, alternative transcripts and expression
RT analysis of CD99L2, a novel paralog of human CD99, and identification of
RT evolutionary conserved motifs.";
RL Gene 307:63-76(2003).
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 -!- TISSUE SPECIFICITY: Expressed predominantly in the ventral medullary
CC surface of the brain, moderate expression in the cerebral cortex and
CC cerebellum. Low expression in lung and kidney. No expression in heart,
CC stomach, intestine and skeletal muscle.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90767.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB031014; BAA90767.1; ALT_FRAME; mRNA.
DR EMBL; AF481858; AAL89685.1; -; mRNA.
DR RefSeq; NP_604454.1; NM_134459.1.
DR RefSeq; XP_006251738.1; XM_006251676.3.
DR RefSeq; XP_008768818.1; XM_008770596.2.
DR RefSeq; XP_017443944.1; XM_017588455.1.
DR AlphaFoldDB; Q8R1R5; -.
DR STRING; 10116.ENSRNOP00000024427; -.
DR PhosphoSitePlus; Q8R1R5; -.
DR SwissPalm; Q8R1R5; -.
DR PaxDb; Q8R1R5; -.
DR PRIDE; Q8R1R5; -.
DR GeneID; 171485; -.
DR UCSC; RGD:620896; rat.
DR CTD; 83692; -.
DR RGD; 620896; Cd99l2.
DR eggNOG; ENOG502RZ6C; Eukaryota.
DR HOGENOM; CLU_092825_0_1_1; -.
DR InParanoid; Q8R1R5; -.
DR OMA; QDDGHRK; -.
DR OrthoDB; 1559463at2759; -.
DR PhylomeDB; Q8R1R5; -.
DR TreeFam; TF332323; -.
DR PRO; PR:Q8R1R5; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000018148; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; Q8R1R5; baseline and differential.
DR Genevisible; Q8R1R5; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050904; P:diapedesis; ISO:RGD.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISO:RGD.
DR GO; GO:2000409; P:positive regulation of T cell extravasation; ISO:RGD.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 1.
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..246
FT /note="CD99 antigen-like protein 2"
FT /id="PRO_0000340095"
FT TOPO_DOM 26..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 26074 MW; D4188C2C0DF11FE4 CRC64;
MVARLTTLLV CLVFSLATLV QRGYGDFDDF NLEDALKETS SVKQSHFSTT TRRTGTTRAP
ANPAERWDHM TTTTTKRPGT TRAPSNPLEL DGFDLEDALD DRNDLDGPKK PSTGEGGGLS
DKDLEDILGG GGYKPDKNKG GGGGYGSQDD PGSGAVTDPG TIAGLVSALA AALLGAVSGY
LSYQHRKFCF SVQRGLDAAY VKGENLEAVV CEEPRVEAAM CEAPPVTDST QHSQPTEPLA
PERPRI
