SORL_RABIT
ID SORL_RABIT Reviewed; 2213 AA.
AC Q95209;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Sortilin-related receptor;
DE AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats;
DE Short=LDLR relative with 11 ligand-binding repeats;
DE Short=LR11 {ECO:0000303|PubMed:8798746};
DE AltName: Full=SorLA-1;
DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats;
DE Short=SorLA;
DE Flags: Precursor;
GN Name=SORL1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP BETA-VLDL.
RC TISSUE=Liver;
RX PubMed=8798746; DOI=10.1074/jbc.271.40.24761;
RA Yamazaki H., Bujo H., Kusunoki J., Seimiya K., Kanaki T., Morisaki N.,
RA Schneider W.J., Saito Y.;
RT "Elements of neural adhesion molecules and a yeast vacuolar protein sorting
RT receptor are present in a novel mammalian low density lipoprotein receptor
RT family member.";
RL J. Biol. Chem. 271:24761-24768(1996).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14764453; DOI=10.1161/01.res.0000120862.79154.0f;
RA Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T.,
RA Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
RT "LR11, an LDL receptor gene family member, is a novel regulator of smooth
RT muscle cell migration.";
RL Circ. Res. 94:752-758(2004).
RN [3]
RP FUNCTION.
RX PubMed=17332490; DOI=10.1161/atvbaha.106.137091;
RA Ohwaki K., Bujo H., Jiang M., Yamazaki H., Schneider W.J., Saito Y.;
RT "A secreted soluble form of LR11, specifically expressed in intimal smooth
RT muscle cells, accelerates formation of lipid-laden macrophages.";
RL Arterioscler. Thromb. Vasc. Biol. 27:1050-1056(2007).
CC -!- FUNCTION: Sorting receptor that directs several proteins to their
CC correct location within the cell. Along with AP-1 complex, involved
CC Golgi apparatus - endosome sorting. Sorting receptor for APP,
CC regulating its intracellular trafficking and processing into
CC amyloidogenic-beta peptides. Retains APP in the trans-Golgi network,
CC hence preventing its transit through late endosomes where amyloid beta
CC peptides Abeta40 and Abeta42 are generated. May also sort newly
CC produced amyloid-beta peptides to lysosomes for catabolism. Does not
CC affect APP trafficking from the endoplasmic reticulum to Golgi
CC compartments. Sorting receptor for the BDNF receptor NTRK2/TRKB that
CC facilitates NTRK2 trafficking between synaptic plasma membranes,
CC postsynaptic densities and cell soma, hence positively regulates BDNF
CC signaling by controlling the intracellular location of its receptor.
CC Sorting receptor for GDNF that promotes GDNF regulated, but not
CC constitutive secretion. Sorting receptor for the GDNF-GFRA1 complex,
CC directing it from the cell surface to endosomes. GDNF is then targeted
CC to lysosomes and degraded, while its receptor GFRA1 recycles back to
CC the cell membrane, resulting in a GDNF clearance pathway. The SORL1-
CC GFRA1 complex further targets RET for endocytosis, but not for
CC degradation, affecting GDNF-induced neurotrophic activities. Sorting
CC receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by
CC promoting its recycling after internalization from endosomes back to
CC the plasma membrane, hence stimulating phosphoinositide 3-kinase
CC (PI3K)-dependent ERBB2 signaling. Sorting receptor for lipoprotein
CC lipase LPL. Promotes LPL localization to endosomes and later to the
CC lysosomes, leading to degradation of newly synthesized LPL. Potential
CC sorting receptor for APOA5, inducing APOA5 internalization to early
CC endosomes, then to late endosomes, wherefrom a portion is sent to
CC lysosomes and degradation, another portion is sorted to the trans-Golgi
CC network. Sorting receptor for the insulin receptor INSR. Promotes
CC recycling of internalized INSR via the Golgi apparatus back to the cell
CC surface, thereby preventing lysosomal INSR catabolism, increasing INSR
CC cell surface expression and strengthening insulin signal reception in
CC adipose tissue. Does not affect INSR internalization (By similarity).
CC Plays a role in renal ion homeostasis, controlling the phospho-
CC regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin
CC A beta phosphatase, possibly through intracellular sorting of STK39 and
CC PPP3CB (By similarity). Stimulates, via the N-terminal ectodomain, the
CC proliferation and migration of smooth muscle cells, possibly by
CC increasing cell surface expression of the urokinase receptor
CC uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence
CC facilitate cell migration. By acting on the migration of intimal smooth
CC muscle cells, may accelerate intimal thickening following vascular
CC injury (PubMed:14764453, PubMed:17332490). Promotes adhesion of
CC monocytes (By similarity). Stimulates proliferation and migration of
CC monocytes/macrophages (PubMed:17332490). Through its action on intimal
CC smooth muscle cells and macrophages, may accelerate intimal thickening
CC and macrophage foam cell formation in the process of atherosclerosis
CC (By similarity). Regulates hypoxia-enhanced adhesion of hematopoietic
CC stem and progenitor cells to the bone marrow stromal cells via a PLAUR-
CC mediated pathway. This function is mediated by the N-terminal
CC ectodomain (By similarity). Metabolic regulator, which functions to
CC maintain the adequate balance between lipid storage and oxidation in
CC response to changing environmental conditions, such as temperature and
CC diet. The N-terminal ectodomain negatively regulates adipose tissue
CC energy expenditure, acting through the inhibition the BMP/Smad pathway
CC (By similarity). May regulate signaling by the heterodimeric
CC neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by
CC promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR
CC and lysosomal degradation. May regulate IL6 signaling, decreasing cis
CC signaling, possibly by interfering with IL6-binding to membrane-bound
CC IL6R, while up-regulating trans signaling via soluble IL6R (By
CC similarity). {ECO:0000250|UniProtKB:O88307,
CC ECO:0000250|UniProtKB:Q92673, ECO:0000269|PubMed:14764453,
CC ECO:0000269|PubMed:17332490}.
CC -!- SUBUNIT: After maturation cleavage, interacts (via N-terminus) with its
CC own propeptide; this interaction prevents interaction with other
CC ligands, including CRLF1, GDNF, GFRA1, IL6 and IL6R. Interacts (via N-
CC terminal ectodomain) with APP, forming a 1:1 stoichiometric complex;
CC this interaction retains APP in the trans-Golgi network and reduces
CC processing into soluble APP-alpha and amyloid-beta peptides. Also
CC interacts with APP C-terminal fragment C99 and with Abeta40. Interacts
CC with beta-secretase BACE1/BACE; this interaction may affect BACE1-
CC binding to APP and hence reduce BACE1-dependent APP cleavage. Interacts
CC with LRPAP1/RAP. Interacts (via C-terminal cytosolic domain) with GGA1
CC and GGA2 (via N-terminal VHS domain). Interacts with PACS1. May
CC interact (via the N-terminal ectodomain) with the morphogenetic
CC neuropeptide, also called head activator or HA; this interaction is
CC impaired in the presence of propeptide. Interacts with neurotensin/NTS.
CC Interacts (via the N-terminal ectodomain) with PDGFB homodimer.
CC Interacts (via N-terminal ectodomain) with the uPA receptor PLAUR.
CC Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in
CC complex with each other, leading to endocytosis. Also interacts with
CC PAI1/SERPINE1 in complex with tPA/PLAT. Interacts (via C-terminus) with
CC AP-1 and AP-2 complexes (By similarity). Interacts with BMPR1A and
CC BMPR1B (By similarity). Interacts with lipoprotein lipase LPL; this
CC interaction is optimal in slightly acidic conditions. Interacts (via N-
CC terminal ectodomain) with GDNF (via propeptide) and GDNF receptor
CC alpha-1/GFRA1, either individually or in complex with each other. The
CC interaction with GDNF occurs mostly intracellularly. Also interacts
CC with other GDNF receptor alpha family members, including GFRA2, GFRA3
CC and GFRA4. Interacts with the insulin receptor INSR; this interaction
CC strongly increases the surface exposure of INSR. Interacts (via
CC cytosolic C-terminus) with STK39/SPAK. Interacts (via N-terminal
CC ectodomain) with the heterodimeric complex CRLF1-CLC; within this
CC complex, the interaction is mediated predominantly by the CRLF1 moiety.
CC Interacts with CNTFR, as well as with the tripartite signaling complex
CC formed by CRLF1, CLC and CNTFR. Interacts (via N-terminal ectodomain)
CC with IL6; this interaction leads to IL6 internalization and lysosomal
CC degradation. Binding of SOLRL1 secreted N-terminal ectodomain to IL6
CC may increase IL6 trans signaling. Interacts with secreted IL6R; this
CC interaction leads to IL6R internalization. Also interacts with
CC transmembrane IL6R; this interaction does not affect subcellular
CC location. Interacts with APOE (By similarity). Interacts with
CC apolipoprotein E-rich beta-VLDL (PubMed:8798746). Interacts with APOA5;
CC this interaction leads to APOA5 internalization and is abolished by
CC heparin. Interaction with APOA5 results in enhanced binding to
CC chylomicrons. Interacts with ROCK2 (By similarity). Interacts (via
CC cytosolic C-terminus) with PPP3CB/calcineurin A beta. Interacts with
CC NTRK2/TRKB; this interaction facilitates NTRK2 trafficking between
CC synaptic plasma membranes, postsynaptic densities and cell soma, hence
CC positively regulates BDNF signaling (By similarity). Interacts (via
CC cytosolic C-terminus) with HSPA12A in an ADP-dependent manner; this
CC interaction affects SORL1 internalization and subcellular localization
CC (By similarity). Interacts (via N-terminal ectodomain) with ERBB2/HER2
CC (By similarity). {ECO:0000250|UniProtKB:O88307,
CC ECO:0000250|UniProtKB:Q92673, ECO:0000269|PubMed:8798746}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:Q92673}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Cell membrane
CC {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q92673}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:Q92673}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:Q92673}. Secreted
CC {ECO:0000269|PubMed:14764453}. Note=Mostly intracellular, predominantly
CC in the trans-Golgi network (TGN) and in endosome, as well as in
CC endosome-to-TGN recycling compartments; found at low levels on the
CC plasma membrane (By similarity). At the cell surface, partially
CC subjected to proteolytic shedding that releases the ectodomain (also
CC called soluble SORLA, solLR11 or sLR11) in the extracellular milieu
CC (PubMed:14764453). The shedding may be catalyzed by ADAM17/TACE.
CC Following shedding, PSEN1/presenilin-1 cleaves the remaining
CC transmembrane fragment and catalyzes the release of a C-terminal
CC fragment in the cytosol and of a soluble N-terminal beta fragment in
CC the extracellular milieu. The C-terminal cytosolic fragment localizes
CC to the nucleus. At the cell surface, the full-length protein undergoes
CC partial clathrin-dependent endocytosis guided by the clathrin adapter
CC protein 2 (AP-2) (By similarity). {ECO:0000250|UniProtKB:Q92673,
CC ECO:0000269|PubMed:14764453}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, in particular the hippocampus,
CC dentate gyrus, and cerebral cortex (at protein level) (PubMed:8798746).
CC Also detected in liver, adrenal glands, pancreas and testis
CC (PubMed:8798746). Expressed in smooth muscle cells, predominantly
CC during proliferation (PubMed:14764453). {ECO:0000269|PubMed:14764453,
CC ECO:0000269|PubMed:8798746}.
CC -!- PTM: Within the Golgi apparatus, the propeptide may be cleaved off by
CC FURIN or a furin-like protease. After cleavage, the propeptide
CC interacts with the mature protein N-terminus, preventing the
CC association with other ligands. At the cell surface, partially
CC subjected to proteolytic shedding that releases the ectodomain in the
CC extracellular milieu. The shedding may be catalyzed by ADAM17/TACE.
CC Following shedding, PSEN1/presenilin-1 cleaves the remaining
CC transmembrane fragment and catalyzes the release of a C-terminal
CC fragment in the cytosol and of a soluble N-terminal beta fragment in
CC the extracellular milieu. The C-terminal cytosolic fragment localizes
CC to the nucleus. {ECO:0000250|UniProtKB:Q92673}.
CC -!- PTM: Phosphorylation at Ser-2205 facilitates the interaction with GGA1.
CC {ECO:0000250|UniProtKB:Q92673}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC subfamily. {ECO:0000305}.
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DR EMBL; D86350; BAA13075.1; -; mRNA.
DR RefSeq; NP_001076133.1; NM_001082664.1.
DR AlphaFoldDB; Q95209; -.
DR BMRB; Q95209; -.
DR SMR; Q95209; -.
DR BioGRID; 1172398; 1.
DR STRING; 9986.ENSOCUP00000009783; -.
DR PRIDE; Q95209; -.
DR GeneID; 100009378; -.
DR KEGG; ocu:100009378; -.
DR CTD; 6653; -.
DR eggNOG; KOG1215; Eukaryota.
DR eggNOG; KOG3511; Eukaryota.
DR InParanoid; Q95209; -.
DR OrthoDB; 1046610at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR GO; GO:0002024; P:diet induced thermogenesis; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0038020; P:insulin receptor recycling; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; ISS:UniProtKB.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:UniProtKB.
DR CDD; cd00063; FN3; 5.
DR CDD; cd00112; LDLa; 11.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 4.10.400.10; -; 11.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00192; LDLa; 11.
DR SMART; SM00135; LY; 5.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF57424; SSF57424; 11.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01209; LDLRA_1; 10.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Disulfide bond; EGF-like domain; Endocytosis; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..81
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033168"
FT CHAIN 82..2213
FT /note="Sortilin-related receptor"
FT /id="PRO_0000033169"
FT TOPO_DOM 82..2136
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2137..2157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2158..2213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 136..147
FT /note="BNR 1"
FT REPEAT 232..243
FT /note="BNR 2"
FT REPEAT 441..452
FT /note="BNR 3"
FT REPEAT 521..532
FT /note="BNR 4"
FT REPEAT 562..573
FT /note="BNR 5"
FT REPEAT 799..842
FT /note="LDL-receptor class B 1"
FT REPEAT 843..886
FT /note="LDL-receptor class B 2"
FT REPEAT 887..929
FT /note="LDL-receptor class B 3"
FT REPEAT 930..971
FT /note="LDL-receptor class B 4"
FT REPEAT 972..1012
FT /note="LDL-receptor class B 5"
FT DOMAIN 1025..1071
FT /note="EGF-like"
FT DOMAIN 1075..1113
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1114..1154
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1155..1193
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1196..1235
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1237..1271
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1272..1316
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1322..1360
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1365..1404
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1416..1454
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1468..1507
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1511..1550
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1556..1648
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1652..1744
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1748..1843
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1842..1926
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1933..2028
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2029..2117
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 2189..2213
FT /note="Required for efficient Golgi apparatus - endosome
FT sorting"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT REGION 2200..2213
FT /note="Required for interaction with GGA1 and GGA2"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT MOTIF 63..65
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2160..2163
FT /note="Potential nuclear localization signal for the C-
FT terminal fragment generated by PSEN1"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT MOTIF 2171..2176
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT MOTIF 2207..2211
FT /note="DXXLL motif involved in the interaction with GGA1"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT MOD_RES 2205
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:Q92673"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1034
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1853
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2091
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1077..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1084..1102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1096..1111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1116..1130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1124..1143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1137..1152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1164..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1176..1191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1198..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1205..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1217..1234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1238..1248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1243..1261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1255..1270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1274..1288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1282..1301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1295..1314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1324..1336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1331..1349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1343..1358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1367..1380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1375..1393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1387..1402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1418..1430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1425..1443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1437..1452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1470..1483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1477..1496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1490..1505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1513..1526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1520..1539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1533..1548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2213 AA; 247766 MW; A54232645A5A0DDA CRC64;
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTRTLHGGRA PLPQERGFRV VQGDPRELRL
WERGDARGAS RADEKPLRRR RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL
ARDSLALARP RSSDVYVSYD YGKSFNKISE KLNFGAGNNT EAVVAQFYHS PADNKRYIFA
DAYAQYLWIT FDFCNTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT
WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF
QLRDKYMFAT KVVHLLGSPL QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF
VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYTPGGAGSD TLVRYFANEP FADFHRVEGL
QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS EGCSLHLAQR
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY
TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKAFTFSEKP VFVYGLLTEP GEKSTVFTIF
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC
FNGEDFDRPV VVSNCSCTRE DYECDFGFRM SEDLALEVCV PDPGFSGKSS PPVPCPVGST
YRRSRGYRKI SGDTCSGGDV EARLEGELVP CPLAEENEFI LYATRKSIHR YDLASGTTEQ
LPLTGLRAAV ALDFDYEHNC LYWSDLALDV IQRLCLNGST GQEVIINSDL ETVEALAFEP
LSQLLYWVDA GFKKIEVANP DGDFRLTVVN SSVLDRPRAL VLVPQEGIMF WTDWGDLKPG
IYRSNMDGSA AYRLVSEDVK WPNGISVDDQ WIYWTDAYLD CIERITFSGQ QRSVILDRLP
HPYAIAVFKN EIYWDDWSQL SIFRASKYSG SQMEILASQL TGLMDMKIFY KGKNTGSNAC
VPRPCSLLCL PRANNSKSCR CPDGVASSVL PSGDLMCDCP KGYELKNNTC VKEEDTCLRN
QYRCSNGNCI NSIWWCDFDN DCGDMSDEKN CPTTICDLDT QFRCQESGTC IPLSYKCDLE
DDCGDNSDER HCEMHQCRSD EYNCSSGMCI RSSWVCDGDN DCRDWSDEAN CTAIYHTCEA
SNFQCRNGHC IPQRWACDGD ADCQDGSDED PANCEKKCNG FRCPNGTCIP STKHCDGLHD
CSDGSDEQHC EPLCTRFMDF VCKNRQQCLF HSMVCDGIIQ CRDGSDEDPA FAGCSRDPEF
HKVCDEFGFQ CQNGVCISLI WKCDGMDDCG DYSDEANCEN PTEAPNCSRY FQFRCDNGHC
IPNRWKCDRE NDCGDWSDEK DCGDSHVLPS TTPAPSTCLP NYYRCGGGAC VIDTWVCDGY
RDCADGSDEE ACPSLPNVTA TSSPSQPGRC DRFEFECHQP KKCIPNWRRC DGHQDCQDGQ
DEANCPTHST LTCMSWEFKC EDGEACIVLS ERCDGFLDCS DESDEKACSD ELTVYKVQNL
QWTADFSGNV TLTWMRPKKM PSAACVYNVY YRVVGESIWK TLETHSNKTN TVLKVLKPDT
TYQVKVQVQC LSKVHNTNDF VTLRTPEGLP DAPQNLQLSL HGEEEGVIVG HWSPPTHTHG
LIREYIVEYS RSGSKVWTSE RAASNFTEIK NLLVNTLYTV RVAAVTSRGI GNWSDSKSIT
TVKGKAIPPP NIHIDNYDEN SLSFTLTVDG NIKVNGYVVN LFWAFDTHKQ EKKTMNFQGS
SVSHKVGNLT AQTAYEISAW AKTDLGDSPL SFEHVTTRGV RPPAPSLKAR AINQTAVECT
WTGPRNVVYG IFYATSFLDL YRNPSSLTTP LHNATVLVGK DEQYLFLVRV VMPYQGPSSD
YVVVKMIPDS RLPPRHLHAV HTGKTSAVIK WESPYDSPDQ DLFYAIAVKD LIRKTDRSYK
VKSRNSTVEY TLSKLEPGGK YHVIVQLGNM SKDASVKITT VSLSAPDALK IITENDHVLL
FWKSLALKEK YFNESRGYEI HMFDSAMNIT AYLGNTTDNF FKISNLKMGH NYTFTVQARC
LLGSQICGEP AVLLYDELGS GGDASAMQAA RSTDVAAVVV PILFLILLSL GVGFAILYTK
HRRLQSSFTA FANSHYSSRL GSAIFSSGDD LGEDDEDAPM ITGFSDDVPM VIA
