ID H9F5V4_MACMU Unreviewed; 469 AA.
AC H9F5V4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Stabilin-1 {ECO:0000313|EMBL:AFE70013.1};
DE Flags: Fragment;
GN Name=STAB1 {ECO:0000313|EMBL:AFE70013.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE70013.1};
RN [1] {ECO:0000313|EMBL:AFE70013.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE70013.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JU326257; AFE70013.1; -; mRNA.
DR AlphaFoldDB; H9F5V4; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd03515; Link_domain_TSG_6_like; 1.
DR Gene3D; 2.30.180.10; FAS1 domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR24038; STABILIN; 1.
DR PANTHER; PTHR24038:SF8; STABILIN-1; 1.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00554; FAS1; 1.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF82153; FAS1 domain; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50213; FAS1; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 375..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..73
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 107..200
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 221..358
FT /note="FAS1"
FT /evidence="ECO:0000259|PROSITE:PS50213"
FT DISULFID 129..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 153..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE70013.1"
SQ SEQUENCE 469 AA; 49412 MW; 725B07A606C1D17D CRC64;
CSEHANCSQV GTVVTCTCLP DYEGDGWSCR ARNPCTDGHR GGCSEHADCL STGLNTRRCE
CHAGYVGDGL QCLEELEPPV DRCLGRPPPC HSDAVCTDLH FQEKRAGVFH LQATSGPYGL
NFSEAEAACK AQGAVLASFP QLSAAQQLGF HLCLMGWLAN GSAAHPVVFP VADCGNGRVG
IVSLGARKNL SERWDAYCFR VQDVACRCRD GFVGDGISTC NGKLLDVLAA TANFSTFYGM
LLGYANATQR GLDFLDFLDD ELTYKTLFVP VNEGFVDNMT LSGPDLELHA SNATLLSANA
SQGKLLPAHS GLSLIISDAG PDNSSWAPVA PGTVVVSHVI VWDIVAFNGI IHALASPLLA
PPQPQAVLAP KAPPVAAGVG AVLAAGALLG LVAGALYLRA QGKPTGFGFS AFQAEEDAAD
DFSPWQEGTN PTLVSVPNPV FGSDTFCEPF HDSLLEEDFP DTQRILTVK
//