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Protein

Sialoadhesin

Gene

Siglec1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a role in hematopoiesis. May act as a counter-receptor for CLEC10A in lymph node.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Sialic acid1 Publication
Binding sitei116 – 1161Sialic acid4 Publications

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • endocytosis Source: UniProtKB-KW
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of T cell apoptotic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Endocytosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Sialoadhesin
Alternative name(s):
Sheep erythrocyte receptor
Short name:
SER
Sialic acid-binding Ig-like lectin 1
Short name:
Siglec-1
CD_antigen: CD169
Gene namesi
Name:Siglec1
Synonyms:Sa, Sn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99668. Siglec1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 16391620ExtracellularSequence analysisAdd
BLAST
Transmembranei1640 – 166021HelicalSequence analysisAdd
BLAST
Topological domaini1661 – 169535CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211W → Q: Loss of sialic acid binding. 1 Publication
Mutagenesisi116 – 1161R → A: Loss of sialic acid binding. 1 Publication
Mutagenesisi116 – 1161R → L: 10-fold loss in affinity to sialic acid. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 16951676SialoadhesinPRO_0000014969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 166PROSITE-ProRule annotation
Disulfide bondi41 ↔ 98PROSITE-ProRule annotation1 Publication
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi160 ↔ 218PROSITE-ProRule annotation
Disulfide bondi263 ↔ 306PROSITE-ProRule annotation
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence analysis
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi347 ↔ 391PROSITE-ProRule annotation
Disulfide bondi434 ↔ 492PROSITE-ProRule annotation
Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi532 ↔ 576PROSITE-ProRule annotation
Glycosylationi583 – 5831N-linked (GlcNAc...)Sequence analysis
Disulfide bondi625 ↔ 685PROSITE-ProRule annotation
Glycosylationi693 – 6931N-linked (GlcNAc...)Sequence analysis
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi725 ↔ 770PROSITE-ProRule annotation
Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi813 ↔ 872PROSITE-ProRule annotation
Glycosylationi882 – 8821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi912 ↔ 956PROSITE-ProRule annotation
Disulfide bondi1001 ↔ 1063PROSITE-ProRule annotation
Glycosylationi1090 – 10901N-linked (GlcNAc...)Sequence analysis
Glycosylationi1100 – 11001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1103 ↔ 1145PROSITE-ProRule annotation
Disulfide bondi1189 ↔ 1237PROSITE-ProRule annotation
Glycosylationi1247 – 12471N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1277 ↔ 1320PROSITE-ProRule annotation
Disulfide bondi1363 ↔ 1422PROSITE-ProRule annotation
Glycosylationi1460 – 14601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1463 ↔ 1509PROSITE-ProRule annotation
Glycosylationi1474 – 14741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1552 ↔ 1611PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ62230.
PaxDbiQ62230.
PRIDEiQ62230.

PTM databases

iPTMnetiQ62230.
PhosphoSiteiQ62230.

Expressioni

Tissue specificityi

Detected in lymph node in the subcapsular sinus, interfollicular regions, and T and B-cell boundary (at protein level). Expressed by macrophages in various tissues. Highest expression in spleen and lymph node with lower amounts in lung, liver, bone marrow, heart and skin. No expression in thymus, kidney, brain or small intestine.1 Publication

Gene expression databases

BgeeiQ62230.

Interactioni

Subunit structurei

Interacts with CLEC10A.5 Publications

Protein-protein interaction databases

BioGridi203360. 1 interaction.
IntActiQ62230. 2 interactions.
MINTiMINT-4135133.
STRINGi10090.ENSMUSP00000028794.

Structurei

Secondary structure

1
1695
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Beta strandi27 – 326Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 443Combined sources
Beta strandi56 – 627Combined sources
Turni63 – 664Combined sources
Beta strandi68 – 747Combined sources
Helixi76 – 783Combined sources
Turni81 – 866Combined sources
Beta strandi87 – 893Combined sources
Helixi93 – 953Combined sources
Beta strandi100 – 1023Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi131 – 1366Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OD7X-ray3.00A20-138[»]
1OD9X-ray2.10A20-138[»]
1ODAX-ray3.31A20-138[»]
1QFOX-ray1.85A/B/C20-138[»]
1QFPX-ray2.80A20-138[»]
1URLX-ray2.40A20-137[»]
2BVEX-ray2.20A/B20-138[»]
ProteinModelPortaliQ62230.
SMRiQ62230. Positions 20-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62230.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 136117Ig-like V-typeAdd
BLAST
Domaini153 – 23583Ig-like C2-type 1Add
BLAST
Domaini239 – 32183Ig-like C2-type 2Add
BLAST
Domaini326 – 40681Ig-like C2-type 3Add
BLAST
Domaini416 – 50893Ig-like C2-type 4Add
BLAST
Domaini509 – 59486Ig-like C2-type 5Add
BLAST
Domaini602 – 701100Ig-like C2-type 6Add
BLAST
Domaini704 – 78178Ig-like C2-type 7Add
BLAST
Domaini795 – 89096Ig-like C2-type 8Add
BLAST
Domaini894 – 97380Ig-like C2-type 9Add
BLAST
Domaini980 – 1079100Ig-like C2-type 10Add
BLAST
Domaini1081 – 116181Ig-like C2-type 11Add
BLAST
Domaini1172 – 126493Ig-like C2-type 12Add
BLAST
Domaini1245 – 133793Ig-like C2-type 13Add
BLAST
Domaini1342 – 143998Ig-like C2-type 14Add
BLAST
Domaini1442 – 152079Ig-like C2-type 15Add
BLAST
Domaini1534 – 162794Ig-like C2-type 16Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1265Sialic acid binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi827 – 8293Cell attachment siteSequence analysis

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDW5. Eukaryota.
ENOG410ZJZH. LUCA.
HOGENOMiHOG000154365.
HOVERGENiHBG003550.
InParanoidiQ62230.
KOiK06548.

Family and domain databases

Gene3Di2.60.40.10. 17 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07679. I-set. 3 hits.
PF00047. ig. 1 hit.
PF13895. Ig_2. 6 hits.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 16 hits.
SM00408. IGc2. 15 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 17 hits.
PROSITEiPS50835. IG_LIKE. 14 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62230-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCVLFSLLLL ASVFSLGQTT WGVSSPKNVQ GLSGSCLLIP CIFSYPADVP
60 70 80 90 100
VSNGITAIWY YDYSGKRQVV IHSGDPKLVD KRFRGRAELM GNMDHKVCNL
110 120 130 140 150
LLKDLKPEDS GTYNFRFEIS DSNRWLDVKG TTVTVTTDPS PPTITIPEEL
160 170 180 190 200
REGMERNFNC STPYLCLQEK QVSLQWRGQD PTHSVTSSFQ SLEPTGVYHQ
210 220 230 240 250
TTLHMALSWQ DHGRTLLCQF SLGAHSSRKE VYLQVPHAPK GVEILLSSSG
260 270 280 290 300
RNILPGDPVT LTCRVNSSYP AVSAVQWARD GVNLGVTGHV LRLFSAAWND
310 320 330 340 350
SGAYTCQATN DMGSLVSSPL SLHVFMAEVK MNPAGPVLEN ETVTLLCSTP
360 370 380 390 400
KEAPQELRYS WYKNHILLED AHASTLHLPA VTRADTGFYF CEVQNAQGSE
410 420 430 440 450
RSSPLSVVVR YPPLTPDLTT FLETQAGLVG ILHCSVVSEP LATVVLSHGG
460 470 480 490 500
LTLASNSGEN DFNPRFRISS APNSLRLEIR DLQPADSGEY TCLAVNSLGN
510 520 530 540 550
STSSLDFYAN VARLLINPSA EVVEGQAVTL SCRSGLSPAP DTRFSWYLNG
560 570 580 590 600
ALLLEGSSSS LLLPAASSTD AGSYYCRTQA GPNTSGPSLP TVLTVFYPPR
610 620 630 640 650
KPTFTARLDL DTSGVGDGRR GILLCHVDSD PPAQLRLLHK GHVVATSLPS
660 670 680 690 700
RCGSCSQRTK VSRTSNSLHV EIQKPVLEDE GVYLCEASNT LGNSSAAASF
710 720 730 740 750
NAKATVLVIT PSNTLREGTE ANLTCNVNQE VAVSPANFSW FRNGVLWTQG
760 770 780 790 800
SLETVRLQPV ARTDAAVYAC RLLTEDGAQL SAPVVLSVLY APDPPKLSAL
810 820 830 840 850
LDVGQGHMAV FICTVDSYPL AHLSLFRGDH LLATNLEPQR PSHGRIQAKA
860 870 880 890 900
TANSLQLEVR ELGLVDSGNY HCEATNILGS ANSSLFFQVR GAWVQVSPSP
910 920 930 940 950
ELREGQAVVL SCQVPTGVSE GTSYSWYQDG RPLQESTSST LRIAAISLRQ
960 970 980 990 1000
AGAYHCQAQA PDTAIASLAA PVSLHVSYTP RHVTLSALLS TDPERLGHLV
1010 1020 1030 1040 1050
CSVQSDPPAQ LQLFHRNRLV ASTLQGADEL AGSNPRLHVT VLPNELRLQI
1060 1070 1080 1090 1100
HFPELEDDGT YTCEASNTLG QASAAADFDA QAVRVTVWPN ATVQEGQQVN
1110 1120 1130 1140 1150
LTCLVWSTHQ DSLSYTWYKG GQQLLGARSI TLPSVKVLDA TSYRCGVGLP
1160 1170 1180 1190 1200
GHAPHLSRPV TLDVLHAPRN LRLTYLLETQ GRQLALVLCT VDSRPPAQLT
1210 1220 1230 1240 1250
LSHGDQLVAS STEASVPNTL RLELQDPRPS NEGLYSCSAH SPLGKANTSL
1260 1270 1280 1290 1300
ELLLEGVRVK MNPSGSVPEG EPVTVTCEDP AALSSALYAW FHNGHWLQEG
1310 1320 1330 1340 1350
PASSLQFLVT TRAHAGAYFC QVHDTQGTRS SRPASLQILY APRDAVLSSF
1360 1370 1380 1390 1400
RDSRTRLMVV IQCTVDSEPP AEMVLSHNGK VLAASHERHS SASGIGHIQV
1410 1420 1430 1440 1450
ARNALRLQVQ DVTLGDGNTY VCTAQNTLGS ISTTQRLLTE TDIRVTAEPG
1460 1470 1480 1490 1500
LDVPEGTALN LSCLLPGGSG PTGNSSFTWF WNRHRLHSAP VPTLSFTPVV
1510 1520 1530 1540 1550
RAQAGLYHCR ADLPTGATTS APVMLRVLYP PKTPTLIVFV EPQGGHQGIL
1560 1570 1580 1590 1600
DCRVDSEPLA ILTLHRGSQL VASNQLHDAP TKPHIRVTAP PNALRVDIEE
1610 1620 1630 1640 1650
LGPSNQGEYV CTASNTLGSA SASAYFGTRA LHQLQLFQRL LWVLGFLAGF
1660 1670 1680 1690
LCLLLGLVAY HTWRKKSSTK LNEDENSAEM ATKKNTIQEE VVAAL
Length:1,695
Mass (Da):182,979
Last modified:September 21, 2011 - v2
Checksum:iAF704F68C40E113A
GO
Isoform 2 (identifier: Q62230-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-340: MAEVKMNPAGPVLEN → SESWMRLRGPVSGKH
     341-1695: Missing.

Show »
Length:340
Mass (Da):37,511
Checksum:i26F3E85E35BC02E9
GO
Isoform 3 (identifier: Q62230-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1529-1599: YPPKTPTLIV...PPNALRVDIE → CEYEPISALC...LLPFWDEYRR
     1600-1695: Missing.

Show »
Length:1,599
Mass (Da):172,769
Checksum:i7FC111F331066F0C
GO

Sequence cautioni

The sequence CAA85268.1 differs from that shown. Reason: Frameshift at positions 895, 897 and 900. Curated
The sequence CAA85290.1 differs from that shown. Reason: Frameshift at positions 895, 897 and 900. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591N → F in AAB95641 (PubMed:9383289).Curated
Sequence conflicti197 – 1971V → S in CAA85268 (PubMed:7925291).Curated
Sequence conflicti197 – 1971V → S in CAA85290 (PubMed:7925291).Curated
Sequence conflicti197 – 1971V → S in AAB95641 (PubMed:9383289).Curated
Sequence conflicti590 – 5901P → Q AA sequence (PubMed:7925291).Curated
Sequence conflicti727 – 7271V → G in CAA85268 (PubMed:7925291).Curated
Sequence conflicti727 – 7271V → G in CAA85290 (PubMed:7925291).Curated
Sequence conflicti727 – 7271V → G in AAB95641 (PubMed:9383289).Curated
Sequence conflicti759 – 7602PV → LL in CAA85268 (PubMed:7925291).Curated
Sequence conflicti759 – 7602PV → LL in CAA85290 (PubMed:7925291).Curated
Sequence conflicti759 – 7602PV → LL in AAB95641 (PubMed:9383289).Curated
Sequence conflicti1050 – 10523IHF → FLV AA sequence (PubMed:7925291).Curated
Sequence conflicti1055 – 10562LE → VQ AA sequence (PubMed:7925291).Curated
Sequence conflicti1062 – 10621T → Q AA sequence (PubMed:7925291).Curated
Sequence conflicti1066 – 10661S → Q AA sequence (PubMed:7925291).Curated
Sequence conflicti1426 – 14261N → H in CAA85268 (PubMed:7925291).Curated
Sequence conflicti1426 – 14261N → H in CAA85290 (PubMed:7925291).Curated
Sequence conflicti1426 – 14261N → H in AAB95641 (PubMed:9383289).Curated
Sequence conflicti1453 – 14531V → W in CAA85268 (PubMed:7925291).Curated
Sequence conflicti1453 – 14531V → W in CAA85290 (PubMed:7925291).Curated
Sequence conflicti1453 – 14531V → W in AAB95641 (PubMed:9383289).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei326 – 34015MAEVK…PVLEN → SESWMRLRGPVSGKH in isoform 2. 1 PublicationVSP_002573Add
BLAST
Alternative sequencei341 – 16951355Missing in isoform 2. 1 PublicationVSP_002574Add
BLAST
Alternative sequencei1529 – 159971YPPKT…RVDIE → CEYEPISALCLSLHLTGPYQ AFSSAQSKGFIGKGLRTLAS SLAGCMWFVSMLGYPALKWR ILLPFWDEYRR in isoform 3. 1 PublicationVSP_002575Add
BLAST
Alternative sequencei1600 – 169596Missing in isoform 3. 1 PublicationVSP_002576Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36293 mRNA. Translation: CAA85290.1. Frameshift.
Z36233 mRNA. Translation: CAA85268.1. Frameshift.
Z36234 mRNA. Translation: CAA85269.1.
U92842
, U92833, U92834, U92836, U92837, U92838, U92839, U92840, U92841 Genomic DNA. Translation: AAB95641.1.
AL831736 Genomic DNA. No translation available.
AL833771 Genomic DNA. No translation available.
PIRiS50065.
RefSeqiNP_035556.3. NM_011426.3.
UniGeneiMm.1374.

Genome annotation databases

GeneIDi20612.
KEGGimmu:20612.
UCSCiuc008mkp.1. mouse. [Q62230-3]
uc008mkq.1. mouse. [Q62230-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Siglec-1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36293 mRNA. Translation: CAA85290.1. Frameshift.
Z36233 mRNA. Translation: CAA85268.1. Frameshift.
Z36234 mRNA. Translation: CAA85269.1.
U92842
, U92833, U92834, U92836, U92837, U92838, U92839, U92840, U92841 Genomic DNA. Translation: AAB95641.1.
AL831736 Genomic DNA. No translation available.
AL833771 Genomic DNA. No translation available.
PIRiS50065.
RefSeqiNP_035556.3. NM_011426.3.
UniGeneiMm.1374.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OD7X-ray3.00A20-138[»]
1OD9X-ray2.10A20-138[»]
1ODAX-ray3.31A20-138[»]
1QFOX-ray1.85A/B/C20-138[»]
1QFPX-ray2.80A20-138[»]
1URLX-ray2.40A20-137[»]
2BVEX-ray2.20A/B20-138[»]
ProteinModelPortaliQ62230.
SMRiQ62230. Positions 20-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203360. 1 interaction.
IntActiQ62230. 2 interactions.
MINTiMINT-4135133.
STRINGi10090.ENSMUSP00000028794.

PTM databases

iPTMnetiQ62230.
PhosphoSiteiQ62230.

Proteomic databases

MaxQBiQ62230.
PaxDbiQ62230.
PRIDEiQ62230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi20612.
KEGGimmu:20612.
UCSCiuc008mkp.1. mouse. [Q62230-3]
uc008mkq.1. mouse. [Q62230-2]

Organism-specific databases

CTDi6614.
MGIiMGI:99668. Siglec1.

Phylogenomic databases

eggNOGiENOG410KDW5. Eukaryota.
ENOG410ZJZH. LUCA.
HOGENOMiHOG000154365.
HOVERGENiHBG003550.
InParanoidiQ62230.
KOiK06548.

Miscellaneous databases

EvolutionaryTraceiQ62230.
PROiQ62230.
SOURCEiSearch...

Gene expression databases

BgeeiQ62230.

Family and domain databases

Gene3Di2.60.40.10. 17 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
PF07679. I-set. 3 hits.
PF00047. ig. 1 hit.
PF13895. Ig_2. 6 hits.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 16 hits.
SM00408. IGc2. 15 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 17 hits.
PROSITEiPS50835. IG_LIKE. 14 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains."
    Crocker P.R., Mucklow S., Boukson V., McWilliam A., Willis A.C., Gordon S., Milon G., Kelm S., Bradfield P.
    EMBO J. 13:4490-4503(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN SEQUENCE.
    Strain: C57BL/6J.
    Tissue: Macrophage.
  2. "Characterization of the mouse sialoadhesin gene, Sn."
    Mucklow S., Gordon S., Crocker P.R.
    Mamm. Genome 8:934-937(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages."
    Crocker P.R.
    EMBO J. 10:1661-1669(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: C57BL/6J.
    Tissue: Spleen.
  5. "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily."
    Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E., Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.
    Curr. Biol. 4:965-972(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIALIC ACID-BINDING.
  6. "CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1)."
    van den Berg T.K., Nath D., Ziltener H.J., Vestweber D., Fukuda M., van Die I., Crocker P.R.
    J. Immunol. 166:3637-3640(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPN.
  7. "Identification of sialoadhesin as a dominant lymph node counter-receptor for mouse macrophage galactose-type C-type lectin 1."
    Kumamoto Y., Higashi N., Denda-Nagai K., Tsuiji M., Sato K., Crocker P.R., Irimura T.
    J. Biol. Chem. 279:49274-49280(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLEC10A, TISSUE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Liver, Pancreas and Spleen.
  9. "Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution."
    May A.P., Robinson R.C., Vinson M., Crocker P.R., Jones E.Y.
    Mol. Cell 1:719-728(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-138 IN COMPLEX WITH 3'SIALYLLACTOSE, DISULFIDE BOND.
  10. "Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis."
    Crocker P.R., Vinson M., Kelm S., Drickamer K.
    Biochem. J. 341:355-361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 20-138, MUTAGENESIS OF TRP-21 AND ARG-116.
  11. "Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin."
    Zaccai N.R., Maenaka K., Maenaka T., Crocker P.R., Brossmer R., Kelm S., Jones E.Y.
    Structure 11:557-567(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-138 IN COMPLEX WITH SIALIC ACID-BASED INHIBITORS, DISULFIDE BOND.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-137 IN COMPLEX WITH SIALIC ACID-CONTAINING PEPTIDE, DISULFIDE BOND.

Entry informationi

Entry nameiSN_MOUSE
AccessioniPrimary (citable) accession number: Q62230
Secondary accession number(s): D3YVZ3
, D3YVZ4, O55216, Q62228, Q62229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 21, 2011
Last modified: June 8, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.