ID A0A2Y9FU31_PHYMC Unreviewed; 702 AA.
AC A0A2Y9FU31;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=CD44 antigen {ECO:0000256|ARBA:ARBA00020474};
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|RefSeq:XP_007129596.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007129596.2};
RN [1] {ECO:0000313|RefSeq:XP_007129596.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007129596.2};
RG RefSeq;
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 RefSeq; XP_007129596.2; XM_007129534.4.
DR AlphaFoldDB; A0A2Y9FU31; -.
DR Ensembl; ENSPCTT00005017706; ENSPCTP00005016044; ENSPCTG00005011079.
DR Proteomes; UP000248484; Chromosome 16.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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..702
FT /note="CD44 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016008352"
FT TRANSMEM 610..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..120
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT REGION 156..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77040 MW; C852DAB25007EBF3 CRC64;
MDTFWWRAAW GLCLVQLSLA QIDLNITCRY AGVFHVEKNG RYSISKTEAA DLCKAFNCTL
PTMAQMEAAL LVGFETCRYG FIDGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPHEEDCT SVTDLPNTFE GPITITIVNR DGTRYTKKGE YRTNPDDINP STAPEEDMSS
GSSSERSTSG GYNIFHTHLP TVYPNPDQDS PWVSSNPETT PATSTDSNII SAGWEPTEEN
EDESDRHPSY SGSGTDDDED FISSTISTTP RVFNDPQQNQ DWTQLSPGHS NPEVSLQTTT
RMTDVDRSST SAYGEKWTQE THSSLSHHGY HDEEETQHPT STTRTPPTST TEETATQKEQ
WFENGWPGEY PQMPKEDSHS TAGTTAASAH DSHPNQRVTM QSQEDRSWTY FFDPVSHPMG
RGHQTERRMD MHTSRSTALQ PSADPNTGLV EDLDRTGPPS VTTQQSGTQS FSTSHGGLEE
DKDHPMTATP TSSNRNDGRG DRRGGNLPED STASVEGYTP YSSDTNEYRT LIPVTPAKTG
SPEVTEVTIV GDSTSNVDLS LPEDQDSSHE PSGRSYTTHG SESAGHSSGS QERGANTTSG
PMRKPQIPEW LIILASLLAL ALILAVCIAV NSRRRCGQKK KLVINNGNGT VEERKPSGLN
GEASKSQEMV HLVNKESSET PDQFVTADER RNLQNVDMKI GV
//