ID F6QYA3_BOVIN Unreviewed; 626 AA.
AC F6QYA3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Myelin associated glycoprotein {ECO:0000313|Ensembl:ENSBTAP00000049802.3};
GN Name=MAG {ECO:0000313|Ensembl:ENSBTAP00000049802.3,
GN ECO:0000313|VGNC:VGNC:31143};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000049802.3, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000049802.3, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000049802.3,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000049802.3}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000049802.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000256|ARBA:ARBA00038361}.
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DR AlphaFoldDB; F6QYA3; -.
DR SMR; F6QYA3; -.
DR STRING; 9913.ENSBTAP00000049802; -.
DR PaxDb; 9913-ENSBTAP00000052366; -.
DR Ensembl; ENSBTAT00000056677.3; ENSBTAP00000049802.3; ENSBTAG00000017044.6.
DR VEuPathDB; HostDB:ENSBTAG00000017044; -.
DR VGNC; VGNC:31143; MAG.
DR GeneTree; ENSGT01100000263535; -.
DR HOGENOM; CLU_020480_1_0_1; -.
DR InParanoid; F6QYA3; -.
DR OMA; KSEYGRC; -.
DR Reactome; R-BTA-193634; Axonal growth inhibition (RHOA activation).
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000017044; Expressed in floor plate of diencephalon and 46 other cell types or tissues.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:1905576; F:ganglioside GT1b binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0033691; F:sialic acid binding; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR CDD; cd00096; Ig; 1.
DR CDD; cd20987; IgC2_CD33_d2_like; 1.
DR CDD; cd05712; IgV_CD33; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR12035:SF107; MYELIN-ASSOCIATED GLYCOPROTEIN; 1.
DR PANTHER; PTHR12035; SIALIC ACID BINDING IMMUNOGLOBULIN-LIKE LECTIN; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..626
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018562373"
FT TRANSMEM 510..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..227
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 239..321
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 329..408
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 573..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 69286 MW; EFE41DE1A9A6D8F4 CRC64;
MIFLTALSLF WIMISASRGG QWGAWMPSSI SAFEGTCVSI PCRFSFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSNLSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIINT PNIVVPPEVM AGTEVEVSCM VPDNCPELHP ELSWLGHEGL
GEPTVLGRLR EEEGTWVQVS LLHFVPTRET NGHRLGCQAS FPNTTLQFEG YASLDIKYPP
VIVEINSTVE AIEGSHVSLF CGADSNPPPL LTWMRDGTVL REAVAESLSL EVDEVTPAED
GVYLCLAENT YGQDNRTVEL SVMYAPWKPM VNGTVVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILATVI YESELQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPVILLESH
CAAARDTVQC LCVVKANPEP SVAFELPLRN VTVNETEREF VYSERSGLLL TSILTLRGQA
QAPPRVICTS HNLYGTKSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESPSFSG GDNPPVVFSS DFRISGAPEK YESERRLGSE RRLLGLRGEP PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK
//
