Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00769
Entry Name
UniProt Accession
Theoretical PI
4.96
Molecular Weight
69352.86
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Myelin-associated glycoprotein
Protein Synonyms/Alias
Brain neuron cytoplasmic protein 3; Sialic acid-binding Ig-like lectin 4a; Siglec-4a;
Gene Name
Mag
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
531
Canonical
AILIAIVCYITQTRR
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Pedraza L, Owens GC, Green LA, Salzer JL. The myelin-associated glycoproteins:membrane disposition, evidence of a novel disulfide linkage betweenimmunoglobulin-like domains, and posttranslational palmitylation. J Cell Biol.1990 Dec;111(6 Pt 1):2651-61.[PMID:1703542]
Functional Description
Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3- linked sialic acid (By similarity).
Sequence Annotation
Topological domain: 20 516 Extracellular.
Transmembrane: 517 536 Helical.
Topological domain: 537 626 Cytoplasmic.
Domain: 22 120 Ig-like V-type.
Domain: 139 237 Ig-like C2-type 1.
Domain: 241 325 Ig-like C2-type 2.
Domain: 327 412 Ig-like C2-type 3.
Domain: 413 508 Ig-like C2-type 4.
Binding site: 118 118 Sialic acid.
Protein Length
626 AA.
Protein Sequence
(Canonical)
MIFLTTLPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY  60
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD  120
LGGYNQYTFS EHSVLDIINT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL  180
GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP  240
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAESLYL DLEEVTPAED  300
GIYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF  360
KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH  420
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTLRGQA  480
QAPPRVICTS RNLYGTQSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK  540
NVTESPSFSA GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGEP PELDLSYSHS  600
DLGKRPTKDS YTLTEELAEY AEIRVK                                       626
FASTA
(Canonical)
>LipidDB-10116-00769|P07722
MIFLTTLPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWY
FNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD
LGGYNQYTFSEHSVLDIINTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL
GEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP
VIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAESLYLDLEEVTPAED
GIYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF
KEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH
CAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTLRGQA
QAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK
NVTESPSFSAGDNPHVLYSPEFRISGAPDKYESEKRLGSERRLLGLRGEPPELDLSYSHS
DLGKRPTKDSYTLTEELAEYAEIRVK
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0033270; C:paranode region of axon; IEA:Ensembl
GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0007155; P:cell adhesion; IEA:UniProtKB-KW
GO:0021762; P:substantia nigra development; IEA:Ensembl
Interpro
InterPro; IPR013162; CD80_C2-set
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR013098; Ig_I-set
InterPro; IPR003599; Ig_sub
InterPro; IPR003598; Ig_sub2
Pfam
Pfam; PF08205; C2-set_2;
Pfam; PF07679; I-set;
SMART
SMART; SM00409; IG;
SMART; SM00408; IGc2;
PROSITE
PROSITE; PS50835; IG_LIKE;
PRINTS