ID G1S8E6_NOMLE Unreviewed; 742 AA.
AC G1S8E6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=CD44 antigen {ECO:0000256|ARBA:ARBA00020474};
DE AltName: Full=Extracellular matrix receptor III {ECO:0000256|ARBA:ARBA00033395};
DE AltName: Full=GP90 lymphocyte homing/adhesion receptor {ECO:0000256|ARBA:ARBA00032514};
DE AltName: Full=HUTCH-I {ECO:0000256|ARBA:ARBA00031823};
DE AltName: Full=Hermes antigen {ECO:0000256|ARBA:ARBA00032917};
DE AltName: Full=Hyaluronate receptor {ECO:0000256|ARBA:ARBA00031179};
DE AltName: Full=Phagocytic glycoprotein 1 {ECO:0000256|ARBA:ARBA00029917};
DE AltName: Full=Phagocytic glycoprotein I {ECO:0000256|ARBA:ARBA00029928};
GN Name=CD44 {ECO:0000313|Ensembl:ENSNLEP00000021785.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000021785.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000021785.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000021785.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR EMBL; ADFV01113414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01113415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003254461.1; XM_003254413.3.
DR AlphaFoldDB; G1S8E6; -.
DR STRING; 61853.ENSNLEP00000021785; -.
DR Ensembl; ENSNLET00000022885.2; ENSNLEP00000021785.1; ENSNLEG00000017932.3.
DR GeneID; 100587652; -.
DR CTD; 960; -.
DR eggNOG; ENOG502RX7Q; Eukaryota.
DR GeneTree; ENSGT00530000063822; -.
DR HOGENOM; CLU_391256_0_0_1; -.
DR InParanoid; G1S8E6; -.
DR OMA; SAYGEKW; -.
DR OrthoDB; 5358652at2759; -.
DR TreeFam; TF334173; -.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:Ensembl.
DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:Ensembl.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl.
DR GO; GO:0070487; P:monocyte aggregation; IEA:Ensembl.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:1900625; P:positive regulation of monocyte aggregation; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
DR CDD; cd03516; Link_domain_CD44_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR001231; CD44_antigen.
DR InterPro; IPR043210; CD44_antigen-like.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR10225:SF6; CD44 ANTIGEN; 1.
DR PANTHER; PTHR10225; HYALURONAN RECEPTOR; 1.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR00658; CD44.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Lectin {ECO:0000256|ARBA:ARBA00023035};
KW Mannose-binding {ECO:0000256|ARBA:ARBA00023035};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..742
FT /note="CD44 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003421546"
FT TRANSMEM 650..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..120
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT REGION 160..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 81657 MW; 459A3011B76B8912 CRC64;
MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL
PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS
GSSSERSSTS GSYIFYTFST VHSIPDEDGP WITDSTDRTP ATTLMSTSAT AAERATKRQE
TWDWFSWLFL PSESKNHLHT TTQMAGTSSN TISAGWEPNE ENEEERERHL SFSGSGIDDD
EDFISSTIST TPRVFDHTKQ NQDWTQRNPS HSNPEVLLQT TTRMTDVDRN GTTAYEGSWN
PEAHSPLIHH EHHEEEETPH STSTIQATPS STMEETATQK EQWFGNRWHE GYRQTPREDS
HLTTGTAAAS AHTSHPMQGR TTPSPEDSSW TDFFDPISHP MGRGHQAGRR MDMDSSHSTT
LQPTANPNTG LVEDLDRTGP LSMTTQQSNS QSFSTSHEGL EEDKDHPTTS TLTSSNRNDV
TGGRRDPNHF EGSTTLLEGY TSHYPHTKES RTFIPVTSVK TGSFGVTEVT VGDSNSNVNH
SLSGDQDAFH PSGGSHTTHG SESAGHSRGS QEGGANTTSG PIRTPQIPEW LIILASLLAL
ALILAVCIAV NSRRRCGQKK KLVINSGNGA VEDRKPSGLN GEASKSQEMV HLVNKESSET
PDQFITADET RNLQNVDMKI GV
//
