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Sortilin-related receptor (Gp250) (Low-density lipoprotein receptor relative with 11 ligand-binding repeats) (LDLR relative with 11 ligand-binding repeats) (LR11) (SorLA-1) (Sorting protein-related receptor containing LDLR class A repeats) (mSorLA)

 SORL_MOUSE              Reviewed;        2215 AA.
O88307; O54711; O70581; Q3UHM3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 157.
RecName: Full=Sortilin-related receptor;
AltName: Full=Gp250;
AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats;
Short=LDLR relative with 11 ligand-binding repeats;
Short=LR11;
AltName: Full=SorLA-1;
AltName: Full=Sorting protein-related receptor containing LDLR class A repeats;
Short=mSorLA;
Flags: Precursor;
Name=Sorl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9726247; DOI=10.1089/dna.1998.17.647;
Kanaki T., Bujo H., Hirayama S., Tanaka K., Yamazaki H., Seimiya K.,
Morisaki N., Schneider W.J., Saito Y.;
"Developmental regulation of LR11 expression in murine brain.";
DNA Cell Biol. 17:647-657(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 183-2215.
TISSUE=Brain;
PubMed=9510025; DOI=10.1016/S0925-4773(97)00177-9;
Hermans-Borgmeyer I., Hampe W., Schinke B., Methner A., Nykjaer A.,
Suesens U., Fenger U., Herbarth B., Schaller H.C.;
"Unique expression pattern of a novel mosaic receptor in the
developing cerebral cortex.";
Mech. Dev. 70:65-76(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1119-1713.
STRAIN=Swiss Webster;
Boehmelt G., Antonio L., Iscove N.N.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=14764453; DOI=10.1161/01.RES.0000120862.79154.0F;
Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S.,
Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
"LR11, an LDL receptor gene family member, is a novel regulator of
smooth muscle cell migration.";
Circ. Res. 94:752-758(2004).
[6]
INTERACTION WITH APP.
PubMed=16174740; DOI=10.1073/pnas.0503689102;
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R.,
Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X.,
Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J.,
Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.;
"Neuronal sorting protein-related receptor sorLA/LR11 regulates
processing of the amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Likely to be a multifunctional endocytic receptor, that
may be implicated in the uptake of lipoproteins and of proteases.
Binds LDL, the major cholesterol-carrying lipoprotein of plasma,
and transports it into cells by endocytosis. Binds the receptor-
associated protein (RAP). Could play a role in cell-cell
interaction. May play a role in neural organization, as well as
the establishment of embryonic organ systems. Involved in APP
trafficking to and from the Golgi apparatus (By similarity). It
probably acts as a sorting receptor that protects APP from
trafficking to late endosome and from processing into amyloid beta
(By similarity). Involved in the regulation of smooth muscle cells
migration, probably through PLAUR binding and decreased
internalization. {ECO:0000250, ECO:0000269|PubMed:14764453}.
-!- SUBUNIT: Interacts with GGA1 and ROCK2 (By similarity). Interacts
with APP. Interacts with PLAUR (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9EQH3:Vps35; NbExp=2; IntAct=EBI-7540114, EBI-775825;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000250}.
Endosome {ECO:0000250}. Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Abundant in brain, where it is mainly
expressed in adult cerebellum, hippocampal ca regions, dentate
gyrus, and to a much lesser extent in the cerebral cortex.
Detectable in kidney, skeletal muscle, lung and spleen, but not in
the liver.
-!- DEVELOPMENTAL STAGE: Expressed as early as embryonic day 6.5
(E6.5) and peaks at E11, the main location is in the CNS during
development. At early stages, it is abundant in a subpopulation of
neurons in the cerebral cortex, in the hippocampus, and granular
and Purkinje cell layers in the cerebellum, whereas in the adult,
expression in cerebellar granular cells and in the cerebral cortex
is low. Expression occurs also in a variety of glands and organs
during organogenesis.
-!- PTM: The propeptide removed in the N-terminus may be cleaved by
furin or homologous proteases. {ECO:0000250}.
-!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
subfamily. {ECO:0000305}.
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EMBL; AB015790; BAA31219.1; -; mRNA.
EMBL; AK147303; BAE27834.1; -; mRNA.
EMBL; AF031816; AAC16739.1; -; mRNA.
EMBL; Y12004; CAA72732.1; -; mRNA.
CCDS; CCDS40594.1; -.
PIR; T00348; T00348.
RefSeq; NP_035566.2; NM_011436.3.
UniGene; Mm.121920; -.
ProteinModelPortal; O88307; -.
SMR; O88307; -.
DIP; DIP-42439N; -.
IntAct; O88307; 1.
MINT; MINT-1342356; -.
STRING; 10090.ENSMUSP00000058613; -.
iPTMnet; O88307; -.
PhosphoSitePlus; O88307; -.
EPD; O88307; -.
MaxQB; O88307; -.
PaxDb; O88307; -.
PeptideAtlas; O88307; -.
PRIDE; O88307; -.
Ensembl; ENSMUST00000060989; ENSMUSP00000058613; ENSMUSG00000049313.
GeneID; 20660; -.
KEGG; mmu:20660; -.
UCSC; uc009pap.1; mouse.
CTD; 6653; -.
MGI; MGI:1202296; Sorl1.
eggNOG; KOG1215; Eukaryota.
eggNOG; KOG3511; Eukaryota.
eggNOG; ENOG410Y3W5; LUCA.
GeneTree; ENSGT00510000046443; -.
HOGENOM; HOG000007009; -.
HOVERGEN; HBG017830; -.
InParanoid; O88307; -.
OMA; EANCPTH; -.
OrthoDB; EOG091G00GS; -.
TreeFam; TF324918; -.
PRO; PR:O88307; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000049313; -.
Genevisible; O88307; MM.
GO; GO:0005769; C:early endosome; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005783; C:endoplasmic reticulum; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0031985; C:Golgi cisterna; ISS:Alzheimers_University_of_Toronto.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005641; C:nuclear envelope lumen; IDA:Alzheimers_University_of_Toronto.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0055037; C:recycling endosome; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005802; C:trans-Golgi network; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030306; F:ADP-ribosylation factor binding; ISO:MGI.
GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902997; P:negative regulation of neurofibrillary tangle assembly; IMP:Alzheimers_University_of_Toronto.
GO; GO:0050768; P:negative regulation of neurogenesis; IMP:Alzheimers_University_of_Toronto.
GO; GO:1901215; P:negative regulation of neuron death; IMP:Alzheimers_University_of_Toronto.
GO; GO:0032091; P:negative regulation of protein binding; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032460; P:negative regulation of protein oligomerization; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902948; P:negative regulation of tau-protein kinase activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902771; P:positive regulation of choline O-acetyltransferase activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902955; P:positive regulation of early endosome to recycling endosome transport; ISS:Alzheimers_University_of_Toronto.
GO; GO:2001137; P:positive regulation of endocytic recycling; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISS:Alzheimers_University_of_Toronto.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISS:Alzheimers_University_of_Toronto.
GO; GO:0051604; P:protein maturation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:Alzheimers_University_of_Toronto.
GO; GO:0006605; P:protein targeting; ISS:Alzheimers_University_of_Toronto.
GO; GO:0000042; P:protein targeting to Golgi; ISS:Alzheimers_University_of_Toronto.
GO; GO:0006622; P:protein targeting to lysosome; ISS:Alzheimers_University_of_Toronto.
GO; GO:0014910; P:regulation of smooth muscle cell migration; ISO:MGI.
CDD; cd00063; FN3; 5.
CDD; cd00112; LDLa; 11.
Gene3D; 2.120.10.30; -; 1.
Gene3D; 2.130.10.10; -; 2.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR031777; Sortilin_C.
InterPro; IPR031778; Sortilin_N.
InterPro; IPR006581; VPS10.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF00041; fn3; 3.
Pfam; PF00057; Ldl_recept_a; 10.
Pfam; PF00058; Ldl_recept_b; 2.
Pfam; PF15902; Sortilin-Vps10; 1.
Pfam; PF15901; Sortilin_C; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00060; FN3; 6.
SMART; SM00192; LDLa; 11.
SMART; SM00135; LY; 5.
SMART; SM00602; VPS10; 1.
SUPFAM; SSF49265; SSF49265; 3.
SUPFAM; SSF57424; SSF57424; 11.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50853; FN3; 4.
PROSITE; PS01209; LDLRA_1; 10.
PROSITE; PS50068; LDLRA_2; 11.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
Cholesterol metabolism; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus;
LDL; Lipid metabolism; Lipid transport; Membrane; Phosphoprotein;
Receptor; Reference proteome; Repeat; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 28 {ECO:0000255}.
PROPEP 29 81 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000033166.
CHAIN 82 2215 Sortilin-related receptor.
/FTId=PRO_0000033167.
TOPO_DOM 82 2138 Extracellular. {ECO:0000255}.
TRANSMEM 2139 2159 Helical. {ECO:0000255}.
TOPO_DOM 2160 2215 Cytoplasmic. {ECO:0000255}.
REPEAT 136 147 BNR 1.
REPEAT 232 243 BNR 2.
REPEAT 441 452 BNR 3.
REPEAT 521 532 BNR 4.
REPEAT 562 573 BNR 5.
REPEAT 800 843 LDL-receptor class B 1.
REPEAT 844 887 LDL-receptor class B 2.
REPEAT 888 932 LDL-receptor class B 3.
REPEAT 933 972 LDL-receptor class B 4.
REPEAT 973 1013 LDL-receptor class B 5.
DOMAIN 1026 1072 EGF-like.
DOMAIN 1076 1114 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1115 1155 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1156 1194 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1198 1236 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1238 1272 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1273 1317 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1323 1361 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1366 1405 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1417 1455 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1469 1508 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1512 1551 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1557 1649 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1653 1745 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1747 1846 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1844 1928 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1935 2030 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 2031 2119 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 2173 2178 Endocytosis signal. {ECO:0000255}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:Q92673}.
MOD_RES 2207 2207 Phosphoserine; by ROCK2.
{ECO:0000250|UniProtKB:Q92673}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 674 674 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 818 818 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 871 871 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1035 1035 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1068 1068 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1164 1164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1191 1191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1246 1246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1367 1367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1458 1458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1608 1608 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1706 1706 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1810 1810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1855 1855 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1895 1895 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1987 1987 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2011 2011 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2055 2055 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2070 2070 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2077 2077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2093 2093 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1078 1090 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1085 1103 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1097 1112 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1117 1131 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1125 1144 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1138 1153 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1158 1170 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1165 1183 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1177 1192 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1199 1211 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1206 1224 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1218 1235 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1239 1249 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1244 1262 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1256 1271 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1275 1289 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1283 1302 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1296 1315 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1325 1337 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1332 1350 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1344 1359 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1368 1381 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1376 1394 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1388 1403 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1419 1431 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1426 1444 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1438 1453 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1471 1484 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1478 1497 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1491 1506 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1514 1527 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1521 1540 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 1534 1549 {ECO:0000255|PROSITE-ProRule:PRU00124}.
CONFLICT 706 706 S -> F (in Ref. 3; AAC16739).
{ECO:0000305}.
CONFLICT 768 768 S -> F (in Ref. 3; AAC16739).
{ECO:0000305}.
CONFLICT 785 785 S -> W (in Ref. 1; BAA31219).
{ECO:0000305}.
CONFLICT 796 796 D -> G (in Ref. 3; AAC16739).
{ECO:0000305}.
CONFLICT 953 953 R -> G (in Ref. 1; BAA31219).
{ECO:0000305}.
CONFLICT 1268 1269 EQ -> DE (in Ref. 1; BAA31219).
{ECO:0000305}.
CONFLICT 1425 1425 H -> A (in Ref. 1; BAA31219).
{ECO:0000305}.
CONFLICT 1425 1425 H -> R (in Ref. 3; AAC16739 and 4;
CAA72732). {ECO:0000305}.
CONFLICT 1468 1468 F -> L (in Ref. 1; BAA31219, 3; AAC16739
and 4; CAA72732). {ECO:0000305}.
CONFLICT 1663 1663 S -> R (in Ref. 1; BAA31219, 3; AAC16739
and 4; CAA72732). {ECO:0000305}.
CONFLICT 1709 1713 EIKNL -> KKKKK (in Ref. 4; CAA72732).
{ECO:0000305}.
CONFLICT 1807 1807 R -> K (in Ref. 1; BAA31219 and 3;
AAC16739). {ECO:0000305}.
CONFLICT 2130 2130 Q -> H (in Ref. 1; BAA31219).
{ECO:0000305}.
SEQUENCE 2215 AA; 247086 MW; 5D7F53806EFE2CB0 CRC64;
MATRSSRRES RLPFLFALVA LLPRGALGGG WTQRLHGGPA PLPQDRGFFV VQGDPRDLRL
GTHGDAPGAS PAARKPLRTR RSAALQPQPI QVYGQVSLND SHNQMVVHWA GEKSNVIVAL
ARDSLALARP KSSDVYVSYD YGKSFSKISE KLNFGVGNNS EAVISQFYHS PADNKRYIFV
DAYAQYLWIT FDFCSTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT
WIMIQEHVKS FSWGIDPYDQ PNAIYIERHE PFGFSTVLRS TDFFQSRENQ EVILEEVRDF
QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY IADAAEDQVF
VCVSHSNNST NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL
QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY
TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF
GSNKESVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC
FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKPY SPPVPCPVGS
SYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAMRKSIY RYDLASGATE
QLPLSGLRAA VALDFDYERN CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE
PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP
GIYRSYMDGS AAYRLVSEDV KWPNGISVDS QWIYWTDAYL DCIERITFSG QQRSVILDSL
PHPYAIAVFK NEIYWDDWSQ LSIFRASKHS RSQVEILASQ LTGLMDMKVF YKGKNAGSNA
CVPQPCSLLC LPKANNSKSC RCPEGVASSV LPSGDLMCDC PQGYQRKNNT CVKEENTCLR
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL
EDDCGDNSDE SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE
ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI PSSKHCDGLR
DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV QCRDGSDEDA AFAGCSQDPE
FHKECDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFHCENGH
CIPNRWKCDR ENDCGDWSDE KDCGDSHVLP SPTPGPSTCL PNYFHCSSGA CVMGTWVCDG
YRDCADGSDE EACPSLANST AASTPTQFGQ CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG
QDEANCPTHS TLTCTSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT STVLKVLKPD
TTYQVKVQVH CLNKVHNTND FVTLRTPEGL PDAPRNLQLS LNSEEEGVIL GHWAPPVHTH
GLIREYIVEY SRSGSKMWAS QRAASNSTEI KNLLLNALYT VRVAAVTSRG IGNWSDSKSI
TTIKGKVIQA PNIHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLSFRG
GSALSHRVSN LTAHTSYEIS AWAKTDLGDS PLAFEHILTR GSSPPAPSLK AKAINQTAVE
CIWTGPKNVV YGIFYATSFL DLYRNPKSVT TSLHNKTVIV SKDEQYLFLV RVLIPYQGPS
SDYVVVKMIP DSRLPPRHLH AVHIGKTSAL IKWESPYDSP DQDLFYAIAV KDLIRKTDRS
YKVRSRNSTV EYSLSKLEPG GKYHIIVQLG NMSKDSSIKI TTVSLSAPDA LKIITENDHV
LLFWKSLALK EKQFNETRGY EIHMSDSAVN LTAYLGNTTD NFFKVSNLKM GHNYTFTVQA
RCLFGSQICG EPAVLLYDEL SSGADAAVIQ AARSTDVAAV VVPILFLILL SLGVGFAILY
TKHRRLQSSF SAFANSHYSS RLGSAIFSSG DDLGEDDEDA PMITGFSDDV PMVIA


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