SN_PIG
ID SN_PIG Reviewed; 1730 AA.
AC A7LCJ3; Q2VF24; Q7YRQ7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Sialoadhesin;
DE Short=pSn;
DE AltName: Full=Sialic acid-binding Ig-like lectin 1;
DE Short=Siglec-1;
DE AltName: Full=p210;
DE Flags: Precursor;
GN Name=SIGLEC1; Synonyms=SA, SN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Alveolar macrophage;
RX PubMed=12857889; DOI=10.1128/jvi.77.15.8207-8215.2003;
RA Vanderheijden N., Delputte P.L., Favoreel H.W., Vandekerckhove J.,
RA Van Damme J., Van Woensel P.A., Nauwynck H.J.;
RT "Involvement of sialoadhesin in entry of porcine reproductive and
RT respiratory syndrome virus into porcine alveolar macrophages.";
RL J. Virol. 77:8207-8215(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19969429; DOI=10.1016/j.vetmic.2009.11.006;
RA An T.Q., Tian Z.J., He Y.X., Xiao Y., Jiang Y.F., Peng J.M., Zhou Y.J.,
RA Liu D., Tong G.Z.;
RT "Porcine reproductive and respiratory syndrome virus attachment is mediated
RT by the N-terminal domain of the sialoadhesin receptor.";
RL Vet. Microbiol. 143:371-378(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu W., Srikumaran S.;
RT "Molecular cloning, sequencing and expression of a porcine sialoadhesin
RT cDNA in macrophages and determination of its role in porcine reproductive
RT and respiratory syndrome.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=10073688; DOI=10.1099/0022-1317-80-2-297;
RA Nauwynck H.J., Duan X., Favoreel H.W., Van Oostveldt P., Pensaert M.B.;
RT "Entry of porcine reproductive and respiratory syndrome virus into porcine
RT alveolar macrophages via receptor-mediated endocytosis.";
RL J. Gen. Virol. 80:297-305(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ARG-116.
RX PubMed=17567703; DOI=10.1128/jvi.00569-07;
RA Delputte P.L., Van Breedam W., Delrue I., Oetke C., Crocker P.R.,
RA Nauwynck H.J.;
RT "Porcine arterivirus attachment to the macrophage-specific receptor
RT sialoadhesin is dependent on the sialic acid-binding activity of the N-
RT terminal immunoglobulin domain of sialoadhesin.";
RL J. Virol. 81:9546-9550(2007).
RN [6]
RP INTERACTION WITH PORCINE REPRODUCTIVE RESPIRATORY SYNDROME VIRUS
RP GLYCOPROTEIN 5.
RX PubMed=20084110; DOI=10.1371/journal.ppat.1000730;
RA Van Breedam W., Van Gorp H., Zhang J.Q., Crocker P.R., Delputte P.L.,
RA Nauwynck H.J.;
RT "The M/GP(5) glycoprotein complex of porcine reproductive and respiratory
RT syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent
RT manner.";
RL PLoS Pathog. 6:E1000730-E1000730(2010).
CC -!- FUNCTION: Macrophage-restricted adhesion molecule that mediates sialic-
CC acid dependent binding to lymphocytes, including granulocytes,
CC monocytes, natural killer cells, B-cells and CD8 T-cells.
CC Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43
CC on T-cells. May play a role in hemopoiesis (By similarity). Acts as an
CC endocytic receptor mediating clathrin dependent endocytosis. In case of
CC porcine reproductive and respiratory syndrome virus (PRRSV), mediates
CC virion attachment and internalization into alveolar macrophages through
CC a clathrin-coated dependent process. {ECO:0000250,
CC ECO:0000269|PubMed:10073688, ECO:0000269|PubMed:12857889,
CC ECO:0000269|PubMed:17567703}.
CC -!- SUBUNIT: Interacts with porcine reproductive respiratory syndrome virus
CC glycoprotein 5. {ECO:0000269|PubMed:20084110}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The sialic acid-binding domain is essential for efficient PRRSV
CC virus attachment and internalization to alveolar macrophages.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
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DR EMBL; AF509585; AAP47136.1; -; mRNA.
DR EMBL; EU003993; ABS19664.1; -; mRNA.
DR EMBL; DQ176853; ABA55712.1; -; mRNA.
DR RefSeq; NP_999511.1; NM_214346.1.
DR AlphaFoldDB; A7LCJ3; -.
DR SMR; A7LCJ3; -.
DR PeptideAtlas; A7LCJ3; -.
DR PRIDE; A7LCJ3; -.
DR GeneID; 397623; -.
DR KEGG; ssc:397623; -.
DR CTD; 6614; -.
DR InParanoid; A7LCJ3; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005769; C:early endosome; IDA:AgBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046790; F:virion binding; IDA:AgBase.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:AgBase.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IMP:AgBase.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:AgBase.
DR GO; GO:0046718; P:viral entry into host cell; IMP:AgBase.
DR Gene3D; 2.60.40.10; -; 17.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 5.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 16.
DR SMART; SM00408; IGc2; 14.
DR SUPFAM; SSF48726; SSF48726; 14.
DR PROSITE; PS50835; IG_LIKE; 15.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Endocytosis; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Immunoglobulin domain; Lectin; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1730
FT /note="Sialoadhesin"
FT /id="PRO_0000398178"
FT TOPO_DOM 20..1642
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1643..1663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1664..1730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..135
FT /note="Ig-like V-type"
FT DOMAIN 139..227
FT /note="Ig-like C2-type 1"
FT DOMAIN 238..316
FT /note="Ig-like C2-type 2"
FT DOMAIN 317..405
FT /note="Ig-like C2-type 3"
FT DOMAIN 415..505
FT /note="Ig-like C2-type 4"
FT DOMAIN 511..593
FT /note="Ig-like C2-type 5"
FT DOMAIN 601..705
FT /note="Ig-like C2-type 6"
FT DOMAIN 708..790
FT /note="Ig-like C2-type 7"
FT DOMAIN 798..893
FT /note="Ig-like C2-type 8"
FT DOMAIN 897..976
FT /note="Ig-like C2-type 9"
FT DOMAIN 983..1082
FT /note="Ig-like C2-type 10"
FT DOMAIN 1083..1165
FT /note="Ig-like C2-type 11"
FT DOMAIN 1172..1257
FT /note="Ig-like C2-type 12"
FT DOMAIN 1259..1335
FT /note="Ig-like C2-type 13"
FT DOMAIN 1346..1442
FT /note="Ig-like C2-type 14"
FT DOMAIN 1443..1529
FT /note="Ig-like C2-type 15"
FT DOMAIN 1537..1630
FT /note="Ig-like C2-type 16"
FT REGION 19..150
FT /note="Necessary for PRRSV virus attachment to alveolar
FT macrophage"
FT BINDING 63
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:Q62230"
FT BINDING 116
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250|UniProtKB:Q62230"
FT BINDING 122..126
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 346..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 433..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 531..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 624..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 729..773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 816..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 915..959
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1004..1066
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1193..1241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1281..1324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1367..1426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1466..1512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1555..1614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 116
FT /note="R->E: Loss of sialic acid binding. Inhibits PRRSV
FT virus attachment and internalization to alveolar
FT macrophages."
FT /evidence="ECO:0000269|PubMed:17567703"
FT CONFLICT 25
FT /note="R -> S (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> V (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="H -> Y (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="C -> Y (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="P -> L (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="S -> L (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="L -> R (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="I -> L (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="N -> S (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> A (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="P -> S (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="R -> Y (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="Q -> H (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="A -> V (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="S -> A (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="H -> R (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="S -> L (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="R -> H (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="H -> R (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="S -> P (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1081
FT /note="L -> F (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="R -> C (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1275
FT /note="A -> T (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1381
FT /note="H -> R (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1390
FT /note="Q -> H (in Ref. 1; AAP47136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="V -> A (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1425
FT /note="V -> I (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1428
FT /note="D -> A (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1468
FT /note="L -> F (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1475
FT /note="I -> M (in Ref. 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1497
FT /note="F -> L (in Ref. 1; AAP47136 and 3; ABA55712)"
FT /evidence="ECO:0000305"
FT CONFLICT 1672
FT /note="H -> Y (in Ref. 1; AAP47136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1730 AA; 184912 MW; A1F1EBB6F33150C7 CRC64;
MDFLLLLLLL ASSALAGLAS WTVSRPETVQ GIKGSCLIIP CTFGFPANVE VPHGITAIWY
YDYSGKRLVV SHSRNPKVVE NHFQGRALLL GQAEQRTCSL LLKDLQPQDS GSYNFRFEIS
EGNRWSDVKG TVVTVTEVPS VPTIALPAKL HEGMEVDFNC STPYVCPTEP VNLQWQGQDP
TRSVTSHLQK LEPSGTSHME TLHMALSWQD HGRILSCQVS AAERRMQKEI HLQVQHAPKG
VEILFSHSGR NVLPGDLVTL SCQVNSSNPQ VSSVQWVKDG TKLKDQKRVL QLRRAAWADA
GVYTCQAGNA VGSSVSPPVS LHVFMAEVQV SPVGSILENQ TVTLACNTPK EAPSELRYSW
CKNHALLEGS HSRTLRLHSV TRADSGFYFC EVQNARGRER SPPVSVVVSH PPLTPDLTAF
PETQAGLVGI LQCSVVSEPP ATLVLSHGGL ISASTSGEGD HSPRFSVASA PNSLRLEIQD
LGPTDSGEYM CSASSSLGNA SSTLDFHANA ARLLISPAAE VVEGQAVTLS CRSSLSLMPD
TRFSWYLNGA LILEGPSSSL LLPAASSTDA GSYHCRAQNS HSTSGPSPPA VLTVLRAPRQ
PVFTAQLDPD TAGAGAGRQG LLLCRVDSDP PAQLQLLHRG RVVASSLSWG GGCCTCGGCF
QRMKVTKAPN LLRVEIRDPA LEDEGVYLCE ASSALGNASA SATLDAQATV LVITPSHTLQ
EGIEANLTCN VSREASGPAN FSWFRDGALW AQGPLDTVTL LPVSRTDAAL YACRIVTEAG
AGLSTPVALN VLYPPDPPKL SALLDVDQGH TAVFVCTVDS HPLAQLALFR GEHLLAASSA
LRLPPRGRLQ AKASANSLQL EVRDLSLGDS GSYHCEATNI LGSANTSLTF QVRGAWVRVS
PSPELQEGQA VVLSCQVPIG VLEGTSYRWY RDGQPLQEST SATLRFAAIT LSQAGAYHCQ
AQASGSATTD LAAPVSLHVT YAPRQATLTT LMDSGLGRLG LLLCRVNSDP PAQLRLLHGS
RLVASTLQGV EELAGSSPRL QVATAPNTLR LEIHNAVLED EGVYTCEATN TLGQTLASAA
LDAQAMRVQV WPNATVQEGQ LVNLTRLVWT THLAQLTYTW YRDQQQLPGA AHSILLPNVT
VTDAASYRCG ILIPGQALRL SRPVALDVLY APRRLRLTHL LESRGGQLAV VLCTVDSRPA
AQLTLSHAGR LLASSTAASV PNTLRLELWE PRPSDEGLYS CSARSPLGQA NTSLELRLEG
VQVALAPSAT VPEGAPVTVT CEDPAARPPT LYVWYHNSRW LQEGSAASLS FPAATRAHAG
AYTCQVQDAQ GTRISQPAAL HILYAPRDAV LSSFWDSRAS PMAVVQCTVD SEPPAEMTLS
HDGKVLATSQ GVHGLAVGTG HVQVARNALQ LRVQNVPSRD KDTYVCMDRN SLGSVSTMGQ
LQPEGVHVVA EPGLDVPEGT ALNLSCRLPS GPGHIGNSTF AWFRNGRQLH TESVPTFTFT
HVARAQAGLY HCQAELPAGA ATSAPVLLRV LYPPKTPTMT VFVEPEGGIQ GILDCRVDSE
PLASLTLHLG SRLVASSQPQ AAPAKPHIRV SASPNALRVD MEELKPSDQG EYVCSASNAL
GSASAATYFG TRALHRLHLF QHLLWFLGLL ASLLFLLLGL GVWYAWRRGN FHKLRMGEYS
VEMVSRKETT QMSTDQEEVT GIGDDAGSVN QAAFDPAHLC ENTQSVKSTV
