SORL_CHICK
ID SORL_CHICK Reviewed; 1592 AA.
AC Q98930;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
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;
DE AltName: Full=SorLA-1;
DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats;
DE Short=SorLA;
DE Flags: Fragment;
GN Name=SORL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9157966; DOI=10.1161/01.atv.17.5.996;
RA Morwald S., Yamazaki H., Bujo H., Kusunoki J., Kanaki T., Seimiya K.,
RA Morisaki N., Nimpf J., Schneider W.J., Saito Y.;
RT "A novel mosaic protein containing LDL receptor elements is highly
RT conserved in humans and chickens.";
RL Arterioscler. Thromb. Vasc. Biol. 17:996-1002(1997).
CC -!- FUNCTION: Sorting receptor that directs numerous proteins to their
CC correct location within the cell. Along with AP-1 complex, involved
CC Golgi apparatus - endosome sorting (By similarity). Sorting receptor
CC for APP, 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 (By similarity). Sorting
CC receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2
CC trafficking between synaptic plasma membranes, postsynaptic densities
CC and cell soma, hence positively regulates BDNF signaling by controlling
CC the intracellular location of its receptor (By similarity). Sorting
CC receptor for GDNF that promotes GDNF regulated, but not constitutive
CC secretion (By similarity). Sorting receptor for ERBB2/HER2. Regulates
CC ERBB2 subcellular distribution by promoting its recycling after
CC internalization from endosomes back to the plasma membrane, hence
CC stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling
CC (By similarity). Sorting receptor for lipoprotein lipase LPL. Promotes
CC LPL localization to endosomes and later to the lysosomes, leading to
CC degradation of newly synthesized LPL (By similarity). Potential sorting
CC receptor for APOA5, inducing APOA5 internalization to early endosomes,
CC then to late endosomes, wherefrom a portion is sent to lysosomes and
CC degradation, another portion is sorted to the trans-Golgi network (By
CC similarity). 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 (By similarity). Plays a role in renal ion homeostasis,
CC possibly through intracellular sorting of STK39 and PPP3CB (By
CC 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, hence facilitating the proteolysis of the extracellular
CC matrix (By similarity). May also stimulate the proliferation, adhesion
CC and migration of monocytes/macrophages (By similarity). Metabolic
CC regulator, which functions to maintain the adequate balance between
CC lipid storage and oxidation in response to changing environmental
CC conditions, such as temperature and diet (By similarity). May regulate
CC signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound
CC to the CNTFR receptor by promoting the endocytosis of the tripartite
CC complex CLCF1-CRLF1-CNTFR and lysosomal degradation (By similarity).
CC May regulate IL6 signaling (By similarity).
CC {ECO:0000250|UniProtKB:O88307, ECO:0000250|UniProtKB:Q92673}.
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:0000250|UniProtKB:Q92673}. Note=Mostly intracellular,
CC predominantly in the trans-Golgi network (TGN) and in endosome, as well
CC as in endosome-to-TGN recycling compartments; found at low levels on
CC the plasma membrane. At the cell surface, partially subjected to
CC proteolytic shedding that releases the ectodomain in the extracellular
CC milieu. Following shedding, may be cleaved the remaining transmembrane
CC fragment and catalyzes the release of a C-terminal fragment in the
CC cytosol and of a soluble N-terminal beta fragment in the extracellular
CC milieu. The C-terminal cytosolic fragment localizes to the nucleus. At
CC the cell surface, the full-length protein undergoes partial clathrin-
CC dependent endocytosis guided by the clathrin adapter protein 2 (AP-2).
CC {ECO:0000250|UniProtKB:Q92673}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, and, at lower levels, in testis
CC and adrenal gland. {ECO:0000269|PubMed:9157966}.
CC -!- PTM: Within the Golgi apparatus, the propeptide is cleaved off by FURIN
CC or a furin-like protease. At the cell surface, partially subjected to
CC proteolytic shedding that releases the ectodomain in the extracellular
CC milieu. Following shedding, may be cleaved the remaining transmembrane
CC fragment and catalyze the release of a C-terminal fragment in the
CC cytosol and of a soluble N-terminal beta fragment in the extracellular
CC milieu. The C-terminal cytosolic fragment localizes to the nucleus.
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; Y08109; CAA69324.1; -; mRNA.
DR AlphaFoldDB; Q98930; -.
DR SMR; Q98930; -.
DR STRING; 9031.ENSGALP00000010625; -.
DR PaxDb; Q98930; -.
DR PRIDE; Q98930; -.
DR VEuPathDB; HostDB:geneid_395998; -.
DR eggNOG; KOG1215; Eukaryota.
DR eggNOG; KOG3511; Eukaryota.
DR InParanoid; Q98930; -.
DR PhylomeDB; Q98930; -.
DR Proteomes; UP000000539; 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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00112; LDLa; 10.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
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; 1.
DR Pfam; PF00057; Ldl_recept_a; 11.
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; SM00192; LDLa; 11.
DR SMART; SM00135; LY; 5.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF57424; SSF57424; 11.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01209; LDLRA_1; 11.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 5.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; EGF-like domain;
KW Endocytosis; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Membrane; Receptor; Reference proteome; Repeat; Secreted;
KW Transport.
FT CHAIN <1..>1592
FT /note="Sortilin-related receptor"
FT /id="PRO_0000064332"
FT REPEAT 43..54
FT /note="BNR 1"
FT REPEAT 139..150
FT /note="BNR 2"
FT REPEAT 348..359
FT /note="BNR 3"
FT REPEAT 428..439
FT /note="BNR 4"
FT REPEAT 469..480
FT /note="BNR 5"
FT REPEAT 707..750
FT /note="LDL-receptor class B 1"
FT REPEAT 751..794
FT /note="LDL-receptor class B 2"
FT REPEAT 795..839
FT /note="LDL-receptor class B 3"
FT REPEAT 840..877
FT /note="LDL-receptor class B 4"
FT REPEAT 878..920
FT /note="LDL-receptor class B 5"
FT DOMAIN 933..979
FT /note="EGF-like"
FT DOMAIN 983..1021
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1022..1062
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1063..1100
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1103..1142
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1144..1179
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1180..1224
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1230..1268
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1273..1312
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1324..1362
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1376..1415
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1419..1457
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1463..1555
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1559..1592
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1152
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 1454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 985..997
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 992..1010
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1004..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1024..1038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1032..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1045..1060
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1065..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1072..1090
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1084..1099
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1105..1117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1112..1130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1124..1141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1145..1155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1150..1168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1162..1177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1182..1196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1190..1209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1203..1222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1232..1244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1239..1257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1251..1266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1275..1288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1283..1301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1295..1310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1326..1338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1333..1351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1345..1360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1378..1391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1385..1404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1398..1413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1421..1433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1427..1446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1440..1455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT NON_TER 1592
SQ SEQUENCE 1592 AA; 178411 MW; 24EDAA5BA231B203 CRC64;
GWVSLNDSHN QMVVHWAGEK SNVIVALARD SLSLLGPKNS DVYISYDYGK SFKKISERFS
FGDGNSSAVA IAQFYHSPAN NQRYIFVDAF VPYLWITTDF CKSIQGFSIP FRAADLLLHS
RNPNLVLGFD RSHPNKQLWK SDDFGQTWIM IQEHVKSFSW GVEPYDKPNT VYIERHEPSG
TSTVIRSTDF FQSRENKEVI LEDVDDFQLR DKYLFATKAV RLLGSLQPSS VQLWVSFNRK
PMRVAQFVTK HPIKEYYIAD ASEDQVFVCV SHDDNRTNLY ISEAEGLKFS LSLENVLYYS
PGGAGSDTLV RYFANEPFAD FHRVEGVRGV YIATLLNGSF SEENMRSVIT FDKGGTWEPL
QPPAETRYGE KTHCELSQGC SLHLAQRLSQ LLNFQLRRMP ILSKESAPGL IIATGSIGKS
MAKKTNVYIS SSAGARWREA LSGPHYYTWG DHGGILVAIA QGTETDQLKY STNEGETWKS
FTFSEKPVFV YGLLTEPGEK STIFTIFGSY KENGHSWLIL QVNTSDVLGV PCTENDYKLW
SPSDERGNEC LLGHKTVFKR RTPHATCFNG EDFDRPVMVS NCSCTREDFE CDFGFKLSED
LSLEVCVPDP EFAGKPYDPP VPCPVGSTYR RTRGYRKISG DTCMGGDIES RLEGEMLPCP
LAEENEFILY ATRYSIHRYD LASGLSQELP LAGLRGAVAL DFDYEHNCLY WADVTLDIIQ
RLCLNGSSGQ EIIISTGLET VEALAFEPLS QLLYWVNAGI PKIEVANPDG DLRLTVLNSS
VLERPRALAL VPREGLMFWT DWGDSRPGIY RSDMDGSLAA CIVSEGVRWP NGISVDDHWI
YWTEAYMDRI ERVDFNGLQR SVILDSLPHP YAIAVFKNEI YWNDWSQLSI FRASKNSGSR
METLVGRLYG IMDMKIFYRG KTTGQNACIA HPCSLLCLPK SNNGRSCKCP EGVSSTVLPS
GEVKCDCPHG YSMKNNTCVK EENTCLPNQY RCFNGNCINS IWQCDNNNDC GDMSDEKNCP
TTVCDAETQF RCRESGTCIP LSYKCDLEDD CGDNSDESHC EAHQCRKDEF SCSSGMCIRL
SWRCDDDNDC RDWSDEANCT MFRTCEASSF QCLNGHCIPQ RWACDGDADC QDGSDEDPTI
CEKKCNGFQC PNGTCISTSK HCNGITDCAD ASDEQDCEIP LCTRYMDFVC KNRQQCLSHS
MVCDGDIQCE DGSDEDANYA GCAQEPEFHR TCDQFSFQCA NGVCISLVWK CDGMDDCGDY
SDEASCENPT DAPTCSRYYQ FQCGNGHCIP NQWKCDGEND CGDWSDEKEC EGSPLLPITT
AVPPTCLPNH FRCGSGACIT NSWVCDGYRD CADGSDEDAC PTSHPNVTSS PPAPRGRCSR
TEFECQQLHK CIPNWKRCDG RRDCQDGTDE RSCPTHSSLS CPQGYRCEDG EACLLATERC
DGYLDCSDGS DERNCTDDTI VYKVQNLQWT ADFSGAITLT WARPKRMSST SCVYNVYYRM
VGESIWKVLE THSNKTSSVL KVLKPDCTYQ VKVQVQCLSR VYNTNDFITL RVPEGLPDAP
FNLQLALKKE AEGVVLCSWS APVNAHGLIR EP
