SORC2_HUMAN
ID SORC2_HUMAN Reviewed; 1159 AA.
AC Q96PQ0; Q9P2L7;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=VPS10 domain-containing receptor SorCS2;
DE Contains:
DE RecName: Full=SorCS2 122 kDa chain {ECO:0000305|PubMed:22155786};
DE Contains:
DE RecName: Full=SorCS2 104 kDa chain {ECO:0000305|PubMed:22155786};
DE Contains:
DE RecName: Full=SorCS2 18 kDa chain {ECO:0000305|PubMed:22155786};
DE Flags: Precursor;
GN Name=SORCS2; Synonyms=KIAA1329;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-451, AND TISSUE SPECIFICITY.
RX PubMed=11499680; DOI=10.1007/s004390100504;
RA Hampe W., Rezgaoui M., Hermans-Borgmeyer I., Schaller H.C.;
RT "The genes for the human VPS10 domain-containing receptors are large and
RT contain many small exons.";
RL Hum. Genet. 108:529-536(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-1159.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP FUNCTION, INTERACTION WITH TRIO; NGF AND NGFR, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=22155786; DOI=10.1126/scisignal.2002060;
RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A.,
RA Chao M.V., Hempstead B.L.;
RT "Neuronal growth cone retraction relies on proneurotrophin receptor
RT signaling through Rac.";
RL Sci. Signal. 4:RA82-RA82(2011).
RN [5]
RP FUNCTION, INTERACTION WITH NGFR; NGF; BDNF AND NTF3, PROTEOLYTIC CLEAVAGE,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF 66-ARG--ARG-69;
RP 116-ARG--ARG-119; THR-1027 AND 1028-LYS--ARG-1029.
RX PubMed=24908487; DOI=10.1016/j.neuron.2014.04.022;
RA Glerup S., Olsen D., Vaegter C.B., Gustafsen C., Sjoegaard S.S., Hermey G.,
RA Kjolby M., Molgaard S., Ulrichsen M., Boggild S., Skeldal S.,
RA Fjorback A.N., Nyengaard J.R., Jacobsen J., Bender D., Bjarkam C.R.,
RA Soerensen E.S., Fuechtbauer E.M., Eichele G., Madsen P., Willnow T.E.,
RA Petersen C.M., Nykjaer A.;
RT "SorCS2 regulates dopaminergic wiring and is processed into an apoptotic
RT two-chain receptor in peripheral glia.";
RL Neuron 82:1074-1087(2014).
RN [6]
RP FUNCTION.
RX PubMed=27457814; DOI=10.1038/mp.2016.108;
RA Glerup S., Bolcho U., Moelgaard S., Boeggild S., Vaegter C.B., Smith A.H.,
RA Nieto-Gonzalez J.L., Ovesen P.L., Pedersen L.F., Fjorback A.N., Kjolby M.,
RA Login H., Holm M.M., Andersen O.M., Nyengaard J.R., Willnow T.E.,
RA Jensen K., Nykjaer A.;
RT "SorCS2 is required for BDNF-dependent plasticity in the hippocampus.";
RL Mol. Psychiatry 21:1740-1751(2016).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28469074; DOI=10.1172/jci.insight.88995;
RA Ma Q., Yang J., Milner T.A., Vonsattel J.G., Palko M.E., Tessarollo L.,
RA Hempstead B.L.;
RT "SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington's
RT disease.";
RL JCI Insight 2:0-0(2017).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=30840898; DOI=10.1016/j.celrep.2019.02.027;
RA Malik A.R., Szydlowska K., Nizinska K., Asaro A., van Vliet E.A., Popp O.,
RA Dittmar G., Fritsche-Guenther R., Kirwan J.A., Nykjaer A., Lukasiuk K.,
RA Aronica E., Willnow T.E.;
RT "SorCS2 Controls Functional Expression of Amino Acid Transporter EAAT3 and
RT Protects Neurons from Oxidative Stress and Epilepsy-Induced Pathology.";
RL Cell Rep. 26:2792-2804(2019).
RN [9]
RP STRUCTURE BY NMR OF 760-869.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PKD domain from human VPS10 domain-containing
RT receptor SORCS2.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: The heterodimer formed by NGFR and SORCS2 functions as
CC receptor for the precursor forms of NGF (proNGF) and BDNF (proBDNF)
CC (PubMed:22155786, PubMed:24908487). ProNGF and proBDNF binding both
CC promote axon growth cone collapse (in vitro) (PubMed:22155786,
CC PubMed:24908487). Plays a role in the regulation of dendritic spine
CC density in hippocampus neurons (By similarity). Required for normal
CC neurite branching and extension in response to BDNF (PubMed:27457814).
CC Plays a role in BDNF-dependent hippocampal synaptic plasticity.
CC Together with NGFR and NTRK2, is required both for BDNF-mediated
CC synaptic long-term depression and long-term potentiation
CC (PubMed:27457814). ProNGF binding promotes dissociation of TRIO from
CC the heterodimer, which leads to inactivation of RAC1 and/or RAC2 and
CC subsequent reorganization of the actin cytoskeleton (PubMed:22155786).
CC Together with the retromer complex subunit VPS35, required for normal
CC expression of GRIN2A at synapses and dendritic cell membranes. Required
CC for normal expression of the amino acid transporter SLC1A1 at the cell
CC membrane, and thereby contributes to protect cells against oxidative
CC stress (By similarity). {ECO:0000250|UniProtKB:Q9EPR5,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487,
CC ECO:0000269|PubMed:27457814}.
CC -!- FUNCTION: [SorCS2 122 kDa chain]: Does not promote Schwann cell
CC apoptosis in response to proBDNF. {ECO:0000269|PubMed:24908487}.
CC -!- FUNCTION: SorCS2 104 kDa chain and SorCS2 18 kDa chain together promote
CC Schwann cell apoptosis in response to proBDNF.
CC {ECO:0000269|PubMed:24908487}.
CC -!- SUBUNIT: Homodimer (in vitro) (By similarity). Heterodimer with NGFR.
CC The extracellular domains of the heterodimer bind the precursor form of
CC NGF (proNGF) (PubMed:22155786, PubMed:24908487). Has much higher
CC affinity for proNGF than for mature NGF (PubMed:24908487). Can also
CC bind mature NGF and BDNF (By similarity). Each chain in the receptor
CC dimer interacts (via extracellular domain) with an NGF dimer (in vitro)
CC (By similarity). Interacts with the precursor forms of BDNF (proBDNF)
CC and NTF3 (proNT3) (PubMed:24908487). The cytoplasmic region of the
CC heterodimer formed by NGFR and SORCS2 binds TRIO. ProNGF binding
CC mediates dissociation of TRIO from the receptor complex
CC (PubMed:22155786). Interacts with SLC1A1. Interacts with VPS35.
CC Interacts (via extracellular domain) with NTRK2 (via extracellular
CC domain). Interacts with VPS35. Interacts (via extracellular domain)
CC with GRIN2A (By similarity). {ECO:0000250|UniProtKB:Q9EPR5,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:24908487}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24908487}. Cell projection
CC {ECO:0000250|UniProtKB:Q9EPR5}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:24908487}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24908487}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9EPR5}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9EPR5}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q9EPR5}. Perikaryon
CC {ECO:0000269|PubMed:28469074}. Cell projection, dendrite
CC {ECO:0000269|PubMed:28469074}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9EPR5}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:Q9EPR5}.
CC -!- TISSUE SPECIFICITY: Detected on neurons in the caudate region
CC (PubMed:28469074). Detected on neurons in the hippocampus (at protein
CC level) (PubMed:30840898). Highly expressed in brain and kidney.
CC Detected at low levels in heart, liver, small intestine, skeletal
CC muscle and thymus (PubMed:11499680). {ECO:0000269|PubMed:11499680,
CC ECO:0000269|PubMed:28469074, ECO:0000269|PubMed:30840898}.
CC -!- PTM: Proteolytic cleavage removes a propeptide, giving rise to a 122
CC kDa chain that includes a cytoplasmic tail. Further cleavage gives rise
CC to a 104 kDa chain that lacks the cytoplasmic tail, and a membrane-
CC bound 18 kDa chain. The 104 kDa chain remains bound to the 18 kDa
CC chain. {ECO:0000269|PubMed:24908487}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:24908487}.
CC -!- MISCELLANEOUS: Expression is decreased in the brains of Huntington
CC disease (HD) patients after the onset of symptoms.
CC {ECO:0000269|PubMed:28469074}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORCS
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The N-terminus of the protein was constructed in analogy to
CC that of the mouse ortholog using the sequence of chromosome 4.
CC {ECO:0000305}.
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DR EMBL; AC004169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF286190; AAL04014.1; -; mRNA.
DR EMBL; AB037750; BAA92567.1; -; mRNA.
DR CCDS; CCDS47008.1; -.
DR RefSeq; NP_065828.2; NM_020777.2.
DR PDB; 1WGO; NMR; -; A=760-869.
DR PDBsum; 1WGO; -.
DR AlphaFoldDB; Q96PQ0; -.
DR SMR; Q96PQ0; -.
DR BioGRID; 121596; 12.
DR IntAct; Q96PQ0; 7.
DR STRING; 9606.ENSP00000422185; -.
DR GlyConnect; 1896; 2 N-Linked glycans (2 sites).
DR GlyGen; Q96PQ0; 8 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q96PQ0; -.
DR PhosphoSitePlus; Q96PQ0; -.
DR SwissPalm; Q96PQ0; -.
DR BioMuta; SORCS2; -.
DR DMDM; 296453015; -.
DR EPD; Q96PQ0; -.
DR jPOST; Q96PQ0; -.
DR MassIVE; Q96PQ0; -.
DR PaxDb; Q96PQ0; -.
DR PeptideAtlas; Q96PQ0; -.
DR PRIDE; Q96PQ0; -.
DR ProteomicsDB; 77727; -.
DR Antibodypedia; 22709; 85 antibodies from 18 providers.
DR DNASU; 57537; -.
DR Ensembl; ENST00000507866.6; ENSP00000422185.2; ENSG00000184985.16.
DR GeneID; 57537; -.
DR KEGG; hsa:57537; -.
DR MANE-Select; ENST00000507866.6; ENSP00000422185.2; NM_020777.3; NP_065828.2.
DR UCSC; uc003gkb.5; human.
DR CTD; 57537; -.
DR DisGeNET; 57537; -.
DR GeneCards; SORCS2; -.
DR HGNC; HGNC:16698; SORCS2.
DR HPA; ENSG00000184985; Tissue enhanced (brain).
DR MIM; 606284; gene.
DR neXtProt; NX_Q96PQ0; -.
DR OpenTargets; ENSG00000184985; -.
DR PharmGKB; PA134902026; -.
DR VEuPathDB; HostDB:ENSG00000184985; -.
DR eggNOG; KOG3511; Eukaryota.
DR GeneTree; ENSGT01030000234563; -.
DR InParanoid; Q96PQ0; -.
DR OMA; SDKRLMA; -.
DR OrthoDB; 1046610at2759; -.
DR PhylomeDB; Q96PQ0; -.
DR TreeFam; TF324918; -.
DR PathwayCommons; Q96PQ0; -.
DR SignaLink; Q96PQ0; -.
DR BioGRID-ORCS; 57537; 8 hits in 1058 CRISPR screens.
DR ChiTaRS; SORCS2; human.
DR EvolutionaryTrace; Q96PQ0; -.
DR GenomeRNAi; 57537; -.
DR Pharos; Q96PQ0; Tbio.
DR PRO; PR:Q96PQ0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96PQ0; protein.
DR Bgee; ENSG00000184985; Expressed in corpus callosum and 137 other tissues.
DR ExpressionAtlas; Q96PQ0; baseline and differential.
DR Genevisible; Q96PQ0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008188; F:neuropeptide receptor activity; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; NAS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00089; PKD; 1.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Endosome; Glycoprotein; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..1159
FT /note="VPS10 domain-containing receptor SorCS2"
FT /id="PRO_0000033172"
FT CHAIN 70..1159
FT /note="SorCS2 122 kDa chain"
FT /evidence="ECO:0000305|PubMed:22155786"
FT /id="PRO_0000447469"
FT CHAIN 120..1030
FT /note="SorCS2 104 kDa chain"
FT /evidence="ECO:0000305|PubMed:22155786"
FT /id="PRO_0000447470"
FT CHAIN 1031..1159
FT /note="SorCS2 18 kDa chain"
FT /evidence="ECO:0000305|PubMed:22155786"
FT /id="PRO_0000447471"
FT TOPO_DOM 51..1078
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1100..1159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 182..193
FT /note="BNR 1"
FT REPEAT 232..243
FT /note="BNR 2"
FT REPEAT 273..284
FT /note="BNR 3"
FT REPEAT 468..479
FT /note="BNR 4"
FT REPEAT 545..556
FT /note="BNR 5"
FT REPEAT 587..598
FT /note="BNR 6"
FT DOMAIN 786..876
FT /note="PKD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 69..70
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:24908487"
FT SITE 119..120
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:24908487"
FT SITE 1030..1031
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:24908487"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 324..329
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 494..499
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 649..684
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 667..699
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 701..760
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 708..725
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT DISULFID 740..775
FT /evidence="ECO:0000250|UniProtKB:Q9EPR5"
FT VARIANT 345
FT /note="G -> R (in dbSNP:rs34058821)"
FT /id="VAR_060109"
FT VARIANT 695
FT /note="T -> M (in dbSNP:rs16840892)"
FT /id="VAR_060110"
FT VARIANT 745
FT /note="T -> I (in dbSNP:rs16840899)"
FT /id="VAR_060111"
FT MUTAGEN 66..69
FT /note="RVPR->AVPA: Decreased proteolytic processing; when
FT associated with 116-A--A-119."
FT /evidence="ECO:0000269|PubMed:24908487"
FT MUTAGEN 116..119
FT /note="RWER->AWEA: Decreased proteolytic processing; when
FT associated with 66-A--A-69."
FT /evidence="ECO:0000269|PubMed:24908487"
FT MUTAGEN 1027
FT /note="T->R: Strongly increases generation of the 104 kDa
FT chain."
FT /evidence="ECO:0000269|PubMed:24908487"
FT MUTAGEN 1028..1030
FT /note="RKR->AKA: Abolishes generation of the 104 kDa
FT chain."
FT /evidence="ECO:0000269|PubMed:24908487"
FT CONFLICT 716
FT /note="S -> P (in Ref. 3; BAA92567)"
FT /evidence="ECO:0000305"
FT STRAND 782..789
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 800..808
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 825..830
FT /evidence="ECO:0007829|PDB:1WGO"
FT HELIX 831..834
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 848..855
FT /evidence="ECO:0007829|PDB:1WGO"
FT STRAND 860..867
FT /evidence="ECO:0007829|PDB:1WGO"
SQ SEQUENCE 1159 AA; 128152 MW; 61DEE8EF428B8B40 CRC64;
MAHRGPSRAS KGPGPTARAP SPGAPPPPRS PRSRPLLLLL LLLGACGAAG RSPEPGRLGP
HAQLTRVPRS PPAGRAEPGG GEDRQARGTE PGAPGPSPGP APGPGEDGAP AAGYRRWERA
APLAGVASRA QVSLISTSFV LKGDATHNQA MVHWTGENSS VILILTKYYH ADMGKVLESS
LWRSSDFGTS YTKLTLQPGV TTVIDNFYIC PTNKRKVILV SSSLSDRDQS LFLSADEGAT
FQKQPIPFFV ETLIFHPKEE DKVLAYTKES KLYVSSDLGK KWTLLQERVT KDHVFWSVSG
VDADPDLVHV EAQDLGGDFR YVTCAIHNCS EKMLTAPFAG PIDHGSLTVQ DDYIFFKATS
ANQTKYYVSY RRNEFVLMKL PKYALPKDLQ IISTDESQVF VAVQEWYQMD TYNLYQSDPR
GVRYALVLQD VRSSRQAEES VLIDILEVRG VKGVFLANQK IDGKVMTLIT YNKGRDWDYL
RPPSMDMNGK PTNCKPPDCH LHLHLRWADN PYVSGTVHTK DTAPGLIMGA GNLGSQLVEY
KEEMYITSDC GHTWRQVFEE EHHILYLDHG GVIVAIKDTS IPLKILKFSV DEGLTWSTHN
FTSTSVFVDG LLSEPGDETL VMTVFGHISF RSDWELVKVD FRPSFSRQCG EEDYSSWELS
NLQGDRCIMG QQRSFRKRKS TSWCIKGRSF TSALTSRVCE CRDSDFLCDY GFERSSSSES
STNKCSANFW FNPLSPPDDC ALGQTYTSSL GYRKVVSNVC EGGVDMQQSQ VQLQCPLTPP
RGLQVSIQGE AVAVRPGEDV LFVVRQEQGD VLTTKYQVDL GDGFKAMYVN LTLTGEPIRH
RYESPGIYRV SVRAENTAGH DEAVLFVQVN SPLQALYLEV VPVIGLNQEV NLTAVLLPLN
PNLTVFYWWI GHSLQPLLSL DNSVTTRFSD TGDVRVTVQA ACGNSVLQDS RVLRVLDQFQ
VMPLQFSKEL DAYNPNTPEW REDVGLVVTR LLSKETSVPQ ELLVTVVKPG LPTLADLYVL
LPPPRPTRKR SLSSDKRLAA IQQVLNAQKI SFLLRGGVRV LVALRDTGTG AEQLGGGGGY
WAVVVLFVIG LFAAGAFILY KFKRKRPGRT VYAQMHNEKE QEMTSPVSHS EDVQGAVQGN
HSGVVLSINS REMHSYLVS
