ID A0A2U4CDG2_TURTR Unreviewed; 676 AA.
AC A0A2U4CDG2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
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_019803473.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019803473.2};
RN [1] {ECO:0000313|RefSeq:XP_019803473.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019803473.2};
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_019803473.2; XM_019947914.2.
DR AlphaFoldDB; A0A2U4CDG2; -.
DR Proteomes; UP000245320; Chromosome 8.
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:UP000245320};
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..676
FT /note="CD44 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030058360"
FT TRANSMEM 584..605
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..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic 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..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 74597 MW; 2E3796B610E00C1B CRC64;
MDTFWWRAAW GLCLVQLSLA QIDLNITCRY KGVFHVEKNG RYSISKTEAA DLCKAFNCTL
PTMAQMEAAL LAGFETCRYG FIDGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPEEDCT SVTDLPNTFE GPITITIVNR DGTRYTKKGE YRTNPDDINP STTPEEDMSS
GSSSERSTSG GYNIFHTHLP TVYPTSDQDS PWVPSNPETT PATTVMSTSG TTSKTATKRQ
GAQDWFFWWF QPSASKIHLH TTTVMAGTDS NIISAGWEAT EENEDESDRH PSYSGSDIDD
DEDFISSTIS TTPRVFNHPQ QNQDWTQPSP GHSNPEVSLQ TTTRMTDVDR SSTSAYGEKW
TQETHSSLSH HGYHDEEETQ HPTSTTRAPP TSTTEETATQ KEQWFENGWP GEYPQMPKED
SHSTAGTTAA SARDSHQNQR VTVQSQEDRS WTYFFDPVSH PMGRGHQTER RMDVDTSHST
TLQPSADPNT GLVEDLDRTG PLSVTTQQSA TQSFSTSRGG LEEDKDHPVT ATPTSSRDRD
SSHDPSGTSY TTHGSESAGH SSGSQDRGAN TTSGPMRKPQ IPEWLIILAS LLALALILAV
CIAVNSRRRC GQKKKLVINN GNGTMEDRKP SGLNGEASKS QEMVHLVNKE STETPDQFMT
ADERRNLQNV DMKIGV
//
