ID A0A340WH64_LIPVE Unreviewed; 745 AA.
AC A0A340WH64;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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_007446380.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007446380.1};
RN [1] {ECO:0000313|RefSeq:XP_007446380.1}
RP IDENTIFICATION.
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_007446380.1; XM_007446318.1.
DR AlphaFoldDB; A0A340WH64; -.
DR STRING; 118797.A0A340WH64; -.
DR GeneID; 103091597; -.
DR KEGG; lve:103091597; -.
DR CTD; 960; -.
DR InParanoid; A0A340WH64; -.
DR OrthoDB; 5358652at2759; -.
DR Proteomes; UP000265300; Unplaced.
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:UP000265300};
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..745
FT /note="CD44 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016420895"
FT TRANSMEM 653..674
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..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 82033 MW; 5D804B5754A7C441 CRC64;
MDTFWWRAAW GLCLVQLSLA QIDLNITCRY KGVFHVEKNG RYSISKTEAA DLCKAFNCTL
PTMAQMEAAL RVGFETCRYG FIDGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPEEDCT SVTDLPNTFE GPITITIVNR DGTRYTKKGE YRTNPDDINP STTPEEDMSS
GSPSERSTSG GYNIFHTHLP TVYPTPDQDS PWVPSNPETT PATTLMSTSG TTSKTATKRQ
EAQDWFSWWF QPSTSKIHLH TTTIMSGTDS NIISAGWEPR EENEDESDRH PSYSGSGIDD
DEDFISSTIS TTPRVFNHPQ QNQDWTQLSP GHSNPGVSLE TTTRMTDVDR SSTSAYGEKW
TQEARSSLSH QGYHDEEETQ HPTSTTRAPP TSTTEETATQ KEQWFENGWP GEYPQRPKED
SHSTAGTTAA SAHDSHQNQR VTMQSQEDRS WTYFFDPVSH PMGRGHQTER RMDMDISHST
TLQPSADPNT GLVEDLDRTG PLSVTTQQSD TQSFSTSHGG LEEDKDHPMT ATPTSSNRND
GTGGRRGGNL PEDSTASVEG YTPYSPDTNE YRTLIPVTPA KTGSPEVTEV TTVGDPTSNV
DLSLSEDQDS SHDPSGRSYT TNGSESAGHS SGSQDRGANT TSGPMRKPQI PEWLIILASL
LALALILAVC IAVNSRRRCG QKKKLVINNG NGTMEERKPS GLNGEASKSQ EMVHLVNKES
SETPDQFMTA DERRNLQNVD MKIGV
//
