ID W5MVY3_LEPOC Unreviewed; 216 AA.
AC W5MVY3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=CD99 antigen-like {ECO:0000313|Ensembl:ENSLOCP00000012542.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012542.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012542.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CD99 family.
CC {ECO:0000256|ARBA:ARBA00008763}.
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DR EMBL; AHAT01012817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01012818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015217208.1; XM_015361722.1.
DR AlphaFoldDB; W5MVY3; -.
DR STRING; 7918.ENSLOCP00000012542; -.
DR Ensembl; ENSLOCT00000012565.1; ENSLOCP00000012542.1; ENSLOCG00000010250.1.
DR GeneID; 102687711; -.
DR KEGG; loc:102687711; -.
DR CTD; 4267; -.
DR eggNOG; ENOG502S70S; Eukaryota.
DR GeneTree; ENSGT00940000154344; -.
DR HOGENOM; CLU_092825_1_1_1; -.
DR InParanoid; W5MVY3; -.
DR OMA; DNQIFSN; -.
DR OrthoDB; 4269940at2759; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000010250; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IBA:GO_Central.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IBA:GO_Central.
DR GO; GO:0072683; P:T cell extravasation; IBA:GO_Central.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076:SF16; CD99 MOLECULE PRECURSOR; 1.
DR PANTHER; PTHR15076; CD99/MIC2 PROTEIN RELATED; 1.
DR Pfam; PF12301; CD99L2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..216
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004868871"
FT REGION 28..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 22115 MW; D0D14596B4DA18C0 CRC64;
MKYLRILLFA ILTIVAQGQD GFDLSDALGG SDPVTAKPKP KPPKDTGTGD FNLGDVFDMP
GPTKPPVTPK PKKPSGDEFD LGDALGGPDP HPTKQPAVPP KNPGKGGSFD NDDLGYVAGE
GDYNPDKGKS GGRSGGRAEG DTQGGSDQPQ AEGSGKIAGI VSAVGVALLG AASSYFAYQK
KKLCFKISGG DPESGNKTQS GTQSEPQILS NLLRSS
//
