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Myelin-associated glycoprotein (Siglec-4a)

 MAG_HUMAN               Reviewed;         626 AA.
P20916; B7Z2E5; F5GYC0; Q15489; Q567S4;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
22-NOV-2017, entry version 178.
RecName: Full=Myelin-associated glycoprotein;
AltName: Full=Siglec-4a;
Flags: Precursor;
Name=MAG; Synonyms=GMA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2476987; DOI=10.1016/0006-291X(89)91145-5;
Sato S., Fujita N., Kurihara T., Kuwano R., Sakimura K., Takahashi Y.,
Miyatake T.;
"cDNA cloning and amino acid sequence for human myelin-associated
glycoprotein.";
Biochem. Biophys. Res. Commun. 163:1473-1480(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=2479762; DOI=10.1002/jnr.490240203;
Spagnol G., Williams M., Srinivasan J., Golier J., Bauer D.,
Lebo R.V., Latov N.;
"Molecular cloning of human myelin-associated glycoprotein.";
J. Neurosci. Res. 24:137-142(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
MET-202.
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 528-626 (ISOFORM 2), ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Brain {ECO:0000312|EMBL:CAA67055.1};
PubMed=9495552; DOI=10.1016/S0169-328X(97)00254-4;
Miescher G.C., Luetzelschwab R., Erne B., Ferracin F., Huber S.,
Steck A.J.;
"Reciprocal expression of myelin-associated glycoprotein splice
variants in the adult human peripheral and central nervous systems.";
Brain Res. Mol. Brain Res. 52:299-306(1997).
[7]
TISSUE SPECIFICITY.
PubMed=6200494; DOI=10.1016/0165-5728(84)90039-0;
Favilla J.T., Frail D.E., Palkovits C.G., Stoner G.L., Braun P.E.,
Webster H.D.;
"Myelin-associated glycoprotein (MAG) distribution in human central
nervous tissue studied immunocytochemically with monoclonal
antibody.";
J. Neuroimmunol. 6:19-30(1984).
[8]
GLYCOSYLATION AT ASN-99; ASN-106; ASN-223; ASN-246; ASN-315; ASN-406;
ASN-450 AND ASN-454, AND LACK OF GLYCOSYLATION AT ASN-332.
PubMed=7505568; DOI=10.1006/bbrc.1993.2501;
Burger D., Pidoux L., Steck A.J.;
"Identification of the glycosylated sequons of human myelin-associated
glycoprotein.";
Biochem. Biophys. Res. Commun. 197:457-464(1993).
[9]
INTERACTION WITH RTN4R.
PubMed=19052207; DOI=10.1523/JNEUROSCI.3828-08.2008;
Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
Strittmatter S.M.;
"Genetic variants of Nogo-66 receptor with possible association to
schizophrenia block myelin inhibition of axon growth.";
J. Neurosci. 28:13161-13172(2008).
[10]
INVOLVEMENT IN SPG75, AND VARIANT SPG75 GLY-430.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
[11]
INVOLVEMENT IN SPG75, VARIANT SPG75 ARG-133, CHARACTERIZATION OF
VARIANT SPG75 ARG-133, SUBCELLULAR LOCATION, TOPOLOGY, AND
GLYCOSYLATION.
PubMed=26179919; DOI=10.1093/brain/awv204;
Lossos A., Elazar N., Lerer I., Schueler-Furman O., Fellig Y.,
Glick B., Zimmerman B.E., Azulay H., Dotan S., Goldberg S.,
Gomori J.M., Ponger P., Newman J.P., Marreed H., Steck A.J.,
Schaeren-Wiemers N., Mor N., Harel M., Geiger T., Eshed-Eisenbach Y.,
Meiner V., Peles E.;
"Myelin-associated glycoprotein gene mutation causes Pelizaeus-
Merzbacher disease-like disorder.";
Brain 138:2521-2536(2015).
[12]
VARIANT SPG75 HIS-118.
PubMed=27606346; DOI=10.1002/acn3.329;
Roda R.H., FitzGibbon E.J., Boucekkine H., Schindler A.B.,
Blackstone C.;
"Neurologic syndrome associated with homozygous mutation at MAG sialic
acid binding site.";
Ann. Clin. Transl. Neurol. 3:650-654(2016).
-!- FUNCTION: Adhesion molecule that mediates interactions between
myelinating cells and neurons by binding to neuronal sialic acid-
containing gangliosides and to the glycoproteins RTN4R and RTN4RL2
(By similarity). Not required for initial myelination, but seems
to play a role in the maintenance of normal axon myelination.
Protects motoneurons against apoptosis, also after injury;
protection against apoptosis is probably mediated via interaction
with neuronal RTN4R and RTN4RL2. Required to prevent degeneration
of myelinated axons in adults; this probably depends on binding to
gangliosides on the axon cell membrane (By similarity). Negative
regulator of neurite outgrowth; in dorsal root ganglion neurons
the inhibition is mediated primarily via binding to neuronal RTN4R
or RTN4RL2 and to a lesser degree via binding to neuronal
gangliosides. In cerebellar granule cells the inhibition is
mediated primarily via binding to neuronal gangliosides. In
sensory neurons, inhibition of neurite extension depends only
partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon
longitudinal growth (By similarity). Inhibits axon outgrowth by
binding to RTN4R (By similarity). Preferentially binds to alpha-
2,3-linked sialic acid. Binds ganglioside Gt1b (By similarity).
{ECO:0000250|UniProtKB:P07722, ECO:0000250|UniProtKB:P20917}.
-!- SUBUNIT: Monomer and homodimer (By similarity). Interacts (via the
first three N-terminal Ig-like domains) with RTN4R and RTN4RL2 (By
similarity). Interacts with RTN4R (PubMed:19052207).
{ECO:0000250|UniProtKB:P07722, ECO:0000250|UniProtKB:P20917,
ECO:0000269|PubMed:19052207}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26179919};
Single-pass type I membrane protein {ECO:0000269|PubMed:26179919}.
Membrane raft {ECO:0000250|UniProtKB:P07722}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=L-MAG {ECO:0000303|PubMed:9495552};
IsoId=P20916-1; Sequence=Displayed;
Name=2; Synonyms=S-MAG {ECO:0000303|PubMed:9495552};
IsoId=P20916-2; Sequence=VSP_042688;
Name=3;
IsoId=P20916-3; Sequence=VSP_045843;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Both isoform 1 and isoform 2 are detected in
myelinated structures in the central and peripheral nervous
system, in periaxonal myelin and at Schmidt-Lanterman incisures
(PubMed:9495552, PubMed:6200494). Detected in optic nerve, in
oligodendroglia and in periaxonal myelin sheaths (PubMed:6200494).
Detected in compact myelin (at protein level) (PubMed:6200494).
Both isoform 1 and isoform 2 are detected in the central and
peripheral nervous system (PubMed:9495552).
{ECO:0000269|PubMed:6200494, ECO:0000269|PubMed:9495552}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:26179919}.
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000250|UniProtKB:P07722}.
-!- DISEASE: Spastic paraplegia 75, autosomal recessive (SPG75)
[MIM:616680]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG75 is characterized by onset in early childhood and
is associated with mild to moderate cognitive impairment.
{ECO:0000269|PubMed:24482476, ECO:0000269|PubMed:26179919,
ECO:0000269|PubMed:27606346}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
(sialic acid binding Ig-like lectin) family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Siglec-4;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_271";
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EMBL; M29273; AAA59545.1; -; mRNA.
EMBL; AK294644; BAH11831.1; -; mRNA.
EMBL; AC002132; AAB58805.1; -; Genomic_DNA.
EMBL; AD000684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053347; AAH53347.1; -; mRNA.
EMBL; BC093045; AAH93045.1; -; mRNA.
EMBL; X98405; CAA67055.1; -; mRNA.
CCDS; CCDS12455.1; -. [P20916-1]
CCDS; CCDS12456.1; -. [P20916-2]
CCDS; CCDS56090.1; -. [P20916-3]
PIR; A61084; A61084.
RefSeq; NP_001186145.1; NM_001199216.1. [P20916-3]
RefSeq; NP_002352.1; NM_002361.3. [P20916-1]
RefSeq; NP_542167.1; NM_080600.2. [P20916-2]
UniGene; Hs.643440; -.
ProteinModelPortal; P20916; -.
SMR; P20916; -.
BioGrid; 110273; 14.
DIP; DIP-58523N; -.
IntAct; P20916; 3.
MINT; MINT-3009422; -.
STRING; 9606.ENSP00000376048; -.
BindingDB; P20916; -.
ChEMBL; CHEMBL5807; -.
iPTMnet; P20916; -.
PhosphoSitePlus; P20916; -.
BioMuta; MAG; -.
DMDM; 126689; -.
PaxDb; P20916; -.
PeptideAtlas; P20916; -.
PRIDE; P20916; -.
Ensembl; ENST00000361922; ENSP00000355234; ENSG00000105695. [P20916-2]
Ensembl; ENST00000392213; ENSP00000376048; ENSG00000105695. [P20916-1]
Ensembl; ENST00000537831; ENSP00000440695; ENSG00000105695. [P20916-3]
GeneID; 4099; -.
KEGG; hsa:4099; -.
UCSC; uc002nyx.3; human. [P20916-1]
CTD; 4099; -.
DisGeNET; 4099; -.
EuPathDB; HostDB:ENSG00000105695.14; -.
GeneCards; MAG; -.
H-InvDB; HIX0080123; -.
HGNC; HGNC:6783; MAG.
HPA; CAB009345; -.
HPA; HPA012499; -.
MalaCards; MAG; -.
MIM; 159460; gene.
MIM; 616680; phenotype.
neXtProt; NX_P20916; -.
OpenTargets; ENSG00000105695; -.
PharmGKB; PA30541; -.
eggNOG; ENOG410IUGJ; Eukaryota.
eggNOG; ENOG410XQVV; LUCA.
GeneTree; ENSGT00760000119139; -.
HOGENOM; HOG000113464; -.
HOVERGEN; HBG006317; -.
InParanoid; P20916; -.
KO; K06771; -.
OMA; CQASFPN; -.
OrthoDB; EOG091G03Q5; -.
PhylomeDB; P20916; -.
TreeFam; TF332441; -.
Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-HSA-210991; Basigin interactions.
SIGNOR; P20916; -.
ChiTaRS; MAG; human.
GeneWiki; Myelin-associated_glycoprotein; -.
GenomeRNAi; 4099; -.
PMAP-CutDB; P20916; -.
PRO; PR:P20916; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105695; -.
CleanEx; HS_MAG; -.
ExpressionAtlas; P20916; baseline and differential.
Genevisible; P20916; HS.
GO; GO:0043218; C:compact myelin; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0097453; C:mesaxon; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:1905576; F:ganglioside GT1b binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0033691; F:sialic acid binding; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF08205; C2-set_2; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein;
Hereditary spastic paraplegia; Immunoglobulin domain; Lectin;
Lipid-binding; Lipoprotein; Membrane; Neurodegeneration; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 19
CHAIN 20 626 Myelin-associated glycoprotein.
/FTId=PRO_0000014856.
TOPO_DOM 20 516 Extracellular. {ECO:0000255}.
TRANSMEM 517 536 Helical. {ECO:0000255}.
TOPO_DOM 537 626 Cytoplasmic. {ECO:0000255}.
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.
REGION 20 325 Interaction with RTN4R and RTN4RL2.
{ECO:0000250|UniProtKB:P07722}.
REGION 65 67 Ganglioside GT1b binding.
{ECO:0000250|UniProtKB:P20917}.
REGION 124 128 Ganglioside GT1b binding.
{ECO:0000250|UniProtKB:P20917}.
REGION 577 626 Required for normal axon myelination in
the central nervous system.
{ECO:0000250|UniProtKB:P20917}.
BINDING 118 118 Ganglioside GT1b.
{ECO:0000250|UniProtKB:P20917}.
SITE 332 332 Not glycosylated.
{ECO:0000269|PubMed:7505568}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:P07722}.
LIPID 531 531 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P07722}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7505568}.
DISULFID 37 165 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 42 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 159 217 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 261 305 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 347 392 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 421 430 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 432 488 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 25 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045843.
VAR_SEQ 574 626 ERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLT
EELAEYAEIRVK -> KEVSTLESH (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9495552}.
/FTId=VSP_042688.
VARIANT 118 118 R -> H (in SPG75; unknown pathological
significance; dbSNP:rs762045079).
{ECO:0000269|PubMed:27606346}.
/FTId=VAR_077495.
VARIANT 133 133 S -> R (in SPG75; alters proper folding;
impairs N-glycosylation; retained in the
endoplasmic reticulum; increased
proteasome-dependent degradation).
{ECO:0000269|PubMed:26179919}.
/FTId=VAR_076224.
VARIANT 202 202 L -> M (in dbSNP:rs11084810).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_059399.
VARIANT 430 430 C -> G (in SPG75; unknown pathological
significance; dbSNP:rs587777229).
{ECO:0000269|PubMed:24482476}.
/FTId=VAR_076225.
CONFLICT 614 614 T -> S (in Ref. 2). {ECO:0000305}.
SEQUENCE 626 AA; 69069 MW; ED2D36B24F21CAAA CRC64;
MIFLTALPLF WIMISASRGG HWGAWMPSSI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSNVSPE LGGKYYFRGD
LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
GEPAVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAS FPNTTLQFEG YASMDVKYPP
VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGTVL REAVAESLLL ELEEVTPAED
GVYACLAENA YGQDNRTVGL SVMYAPWKPT VNGTMVAVEG ETVSILCSTQ SNPDPILTIF
KEKQILSTVI YESELQLELP AVSPEDDGEY WCVAENQYGQ RATAFNLSVE FAPVLLLESH
CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNESEREF VYSERSGLVL TSILTLRGQA
QAPPRVICTA RNLYGAKSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
NVTESPSFSA GDNPPVLFSS DFRISGAPEK YESERRLGSE RRLLGLRGEP PELDLSYSHS
DLGKRPTKDS YTLTEELAEY AEIRVK


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