PLXB2_HUMAN
ID PLXB2_HUMAN Reviewed; 1838 AA.
AC O15031; A6QRH0; Q7KZU3; Q9BSU7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Plexin-B2;
DE AltName: Full=MM1;
DE Flags: Precursor;
GN Name=PLXNB2; Synonyms=KIAA0315;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1364-1838.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1369-1838.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ARHGEF11 AND ARHGEF12, AND FUNCTION.
RX PubMed=12183458; DOI=10.1074/jbc.m206005200;
RA Perrot V., Vazquez-Prado J., Gutkind J.S.;
RT "Plexin B regulates Rho through the guanine nucleotide exchange factors
RT leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF.";
RL J. Biol. Chem. 277:43115-43120(2002).
RN [6]
RP SUBUNIT, HETERODIMERIZATION WITH PLXNB1, MUTAGENESIS OF 1161-ARG--ARG-1164,
RP PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=12533544; DOI=10.1074/jbc.m210156200;
RA Artigiani S., Barberis D., Fazzari P., Longati P., Angelini P.,
RA van de Loo J.-W., Comoglio P.M., Tamagnone L.;
RT "Functional regulation of semaphorin receptors by proprotein convertases.";
RL J. Biol. Chem. 278:10094-10101(2003).
RN [7]
RP INTERACTION WITH MET AND MST1R, AND FUNCTION.
RX PubMed=15184888; DOI=10.1038/sj.onc.1207650;
RA Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.;
RT "Interplay between scatter factor receptors and B plexins controls invasive
RT growth.";
RL Oncogene 23:5131-5137(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127 AND ASN-733.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-318, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that
CC plays an important role in cell-cell signaling (By similarity). Plays a
CC role in glutamatergic synapse development and is required for SEMA4A-
CC mediated excitatory synapse development (By similarity). Binding to
CC class 4 semaphorins promotes downstream activation of RHOA and
CC phosphorylation of ERBB2 at 'Tyr-1248' (By similarity). Required for
CC normal differentiation and migration of neuronal cells during brain
CC corticogenesis and for normal embryonic brain development (By
CC similarity). Regulates the migration of cerebellar granule cells in the
CC developing brain (By similarity). Plays a role in RHOA activation and
CC subsequent changes of the actin cytoskeleton (PubMed:12183458). Plays a
CC role in axon guidance, invasive growth and cell migration
CC (PubMed:15184888). May modulate the activity of RAC1 and CDC42 (By
CC similarity). {ECO:0000250|UniProtKB:B2RXS4,
CC ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:15184888}.
CC -!- SUBUNIT: Monomer, and heterodimer with PLXNB1 (PubMed:12533544).
CC Interacts with SEMA4C, SEMA4D and SEMA4G (By similarity). Interacts
CC with MET (PubMed:15184888). Interacts with ARHGEF11 and ARHGEF12
CC (PubMed:12183458). May also interact with MST1R (PubMed:15184888).
CC {ECO:0000250|UniProtKB:B2RXS4, ECO:0000269|PubMed:12183458,
CC ECO:0000269|PubMed:12533544, ECO:0000269|PubMed:15184888}.
CC -!- INTERACTION:
CC O15031; P08581: MET; NbExp=2; IntAct=EBI-722004, EBI-1039152;
CC O15031; Q04912: MST1R; NbExp=2; IntAct=EBI-722004, EBI-2637518;
CC O15031; Q92730: RND1; NbExp=2; IntAct=EBI-722004, EBI-448618;
CC O15031; P52198: RND2; NbExp=2; IntAct=EBI-722004, EBI-1111436;
CC O15031; P61587: RND3; NbExp=2; IntAct=EBI-722004, EBI-1111534;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12533544};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002313; BAA21571.1; ALT_INIT; mRNA.
DR EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004542; AAH04542.2; -; mRNA.
DR EMBL; BT006887; AAP35533.1; -; mRNA.
DR CCDS; CCDS43035.1; -.
DR RefSeq; NP_036533.2; NM_012401.3.
DR RefSeq; XP_005261966.1; XM_005261909.1.
DR RefSeq; XP_005261967.1; XM_005261910.2.
DR RefSeq; XP_005261968.1; XM_005261911.4.
DR RefSeq; XP_006724476.1; XM_006724413.2.
DR RefSeq; XP_016884192.1; XM_017028703.1.
DR RefSeq; XP_016884193.1; XM_017028704.1.
DR PDB; 4E71; X-ray; 2.26 A; A=1452-1562.
DR PDBsum; 4E71; -.
DR AlphaFoldDB; O15031; -.
DR SMR; O15031; -.
DR BioGRID; 117178; 215.
DR IntAct; O15031; 44.
DR MINT; O15031; -.
DR STRING; 9606.ENSP00000409171; -.
DR GlyConnect; 1613; 57 N-Linked glycans (11 sites).
DR GlyGen; O15031; 16 sites, 56 N-linked glycans (11 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O15031; -.
DR PhosphoSitePlus; O15031; -.
DR SwissPalm; O15031; -.
DR BioMuta; PLXNB2; -.
DR CPTAC; CPTAC-1504; -.
DR CPTAC; CPTAC-2603; -.
DR EPD; O15031; -.
DR jPOST; O15031; -.
DR MassIVE; O15031; -.
DR MaxQB; O15031; -.
DR PaxDb; O15031; -.
DR PeptideAtlas; O15031; -.
DR PRIDE; O15031; -.
DR ProteomicsDB; 48388; -.
DR Antibodypedia; 322; 153 antibodies from 22 providers.
DR DNASU; 23654; -.
DR Ensembl; ENST00000359337.9; ENSP00000352288.4; ENSG00000196576.16.
DR Ensembl; ENST00000449103.5; ENSP00000409171.1; ENSG00000196576.16.
DR GeneID; 23654; -.
DR KEGG; hsa:23654; -.
DR MANE-Select; ENST00000359337.9; ENSP00000352288.4; NM_012401.4; NP_036533.2.
DR UCSC; uc003bkv.4; human.
DR CTD; 23654; -.
DR DisGeNET; 23654; -.
DR GeneCards; PLXNB2; -.
DR HGNC; HGNC:9104; PLXNB2.
DR HPA; ENSG00000196576; Low tissue specificity.
DR MIM; 604293; gene.
DR neXtProt; NX_O15031; -.
DR OpenTargets; ENSG00000196576; -.
DR PharmGKB; PA33430; -.
DR VEuPathDB; HostDB:ENSG00000196576; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_0_1; -.
DR InParanoid; O15031; -.
DR OMA; CTPPIDE; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; O15031; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; O15031; -.
DR SignaLink; O15031; -.
DR BioGRID-ORCS; 23654; 23 hits in 1077 CRISPR screens.
DR ChiTaRS; PLXNB2; human.
DR GeneWiki; PLXNB2; -.
DR GenomeRNAi; 23654; -.
DR Pharos; O15031; Tbio.
DR PRO; PR:O15031; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O15031; protein.
DR Bgee; ENSG00000196576; Expressed in right uterine tube and 182 other tissues.
DR ExpressionAtlas; O15031; baseline and differential.
DR Genevisible; O15031; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:1904861; P:excitatory synapse assembly; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IMP:CACAO.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Developmental protein; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1838
FT /note="Plexin-B2"
FT /id="PRO_0000024673"
FT TOPO_DOM 20..1197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1198..1218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1219..1838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..466
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 803..893
FT /note="IPT/TIG 1"
FT DOMAIN 895..980
FT /note="IPT/TIG 2"
FT DOMAIN 983..1092
FT /note="IPT/TIG 3"
FT SITE 1164..1165
FT /note="Cleavage; by proprotein convertases"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RXS4"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RXS4"
FT MOD_RES 1570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RXS4"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 112..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 250..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 266..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 330..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 469..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 475..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 478..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 489..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 555..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VARIANT 318
FT /note="K -> E (in dbSNP:rs28379706)"
FT /evidence="ECO:0007744|PubMed:24275569"
FT /id="VAR_050600"
FT VARIANT 823
FT /note="I -> V (in dbSNP:rs11547731)"
FT /id="VAR_061537"
FT MUTAGEN 1161..1164
FT /note="RQKR->AQKA: Abolishes cleavage by proprotein
FT convertases."
FT /evidence="ECO:0000269|PubMed:12533544"
FT CONFLICT 1535
FT /note="R -> Q (in Ref. 3; AAH04542 and 4; AAP35533)"
FT /evidence="ECO:0000305"
FT STRAND 1462..1469
FT /evidence="ECO:0007829|PDB:4E71"
FT STRAND 1477..1482
FT /evidence="ECO:0007829|PDB:4E71"
FT HELIX 1487..1498
FT /evidence="ECO:0007829|PDB:4E71"
FT STRAND 1512..1517
FT /evidence="ECO:0007829|PDB:4E71"
FT HELIX 1545..1548
FT /evidence="ECO:0007829|PDB:4E71"
FT STRAND 1555..1560
FT /evidence="ECO:0007829|PDB:4E71"
SQ SEQUENCE 1838 AA; 205127 MW; 4AE43003828BC769 CRC64;
MALQLWALTL LGLLGAGASL RPRKLDFFRS EKELNHLAVD EASGVVYLGA VNALYQLDAK
LQLEQQVATG PALDNKKCTP PIEASQCHEA EMTDNVNQLL LLDPPRKRLV ECGSLFKGIC
ALRALSNISL RLFYEDGSGE KSFVASNDEG VATVGLVSST GPGGDRVLFV GKGNGPHDNG
IIVSTRLLDR TDSREAFEAY TDHATYKAGY LSTNTQQFVA AFEDGPYVFF VFNQQDKHPA
RNRTLLARMC REDPNYYSYL EMDLQCRDPD IHAAAFGTCL AASVAAPGSG RVLYAVFSRD
SRSSGGPGAG LCLFPLDKVH AKMEANRNAC YTGTREARDI FYKPFHGDIQ CGGHAPGSSK
SFPCGSEHLP YPLGSRDGLR GTAVLQRGGL NLTAVTVAAE NNHTVAFLGT SDGRILKVYL
TPDGTSSEYD SILVEINKRV KRDLVLSGDL GSLYAMTQDK VFRLPVQECL SYPTCTQCRD
SQDPYCGWCV VEGRCTRKAE CPRAEEASHW LWSRSKSCVA VTSAQPQNMS RRAQGEVQLT
VSPLPALSEE DELLCLFGES PPHPARVEGE AVICNSPSSI PVTPPGQDHV AVTIQLLLRR
GNIFLTSYQY PFYDCRQAMS LEENLPCISC VSNRWTCQWD LRYHECREAS PNPEDGIVRA
HMEDSCPQFL GPSPLVIPMN HETDVNFQGK NLDTVKGSSL HVGSDLLKFM EPVTMQESGT
FAFRTPKLSH DANETLPLHL YVKSYGKNID SKLHVTLYNC SFGRSDCSLC RAANPDYRCA
WCGGQSRCVY EALCNTTSEC PPPVITRIQP ETGPLGGGIR ITILGSNLGV QAGDIQRISV
AGRNCSFQPE RYSVSTRIVC VIEAAETPFT GGVEVDVFGK LGRSPPNVQF TFQQPKPLSV
EPQQGPQAGG TTLTIHGTHL DTGSQEDVRV TLNGVPCKVT KFGAQLQCVT GPQATRGQML
LEVSYGGSPV PNPGIFFTYR ENPVLRAFEP LRSFASGGRS INVTGQGFSL IQRFAMVVIA
EPLQSWQPPR EAESLQPMTV VGTDYVFHND TKVVFLSPAV PEEPEAYNLT VLIEMDGHRA
LLRTEAGAFE YVPDPTFENF TGGVKKQVNK LIHARGTNLN KAMTLQEAEA FVGAERCTMK
TLTETDLYCE PPEVQPPPKR RQKRDTTHNL PEFIVKFGSR EWVLGRVEYD TRVSDVPLSL
ILPLVIVPMV VVIAVSVYCY WRKSQQAERE YEKIKSQLEG LEESVRDRCK KEFTDLMIEM
EDQTNDVHEA GIPVLDYKTY TDRVFFLPSK DGDKDVMITG KLDIPEPRRP VVEQALYQFS
NLLNSKSFLI NFIHTLENQR EFSARAKVYF ASLLTVALHG KLEYYTDIMH TLFLELLEQY
VVAKNPKLML RRSETVVERM LSNWMSICLY QYLKDSAGEP LYKLFKAIKH QVEKGPVDAV
QKKAKYTLND TGLLGDDVEY APLTVSVIVQ DEGVDAIPVK VLNCDTISQV KEKIIDQVYR
GQPCSCWPRP DSVVLEWRPG STAQILSDLD LTSQREGRWK RVNTLMHYNV RDGATLILSK
VGVSQQPEDS QQDLPGERHA LLEEENRVWH LVRPTDEVDE GKSKRGSVKE KERTKAITEI
YLTRLLSVKG TLQQFVDNFF QSVLAPGHAV PPAVKYFFDF LDEQAEKHNI QDEDTIHIWK
TNSLPLRFWV NILKNPHFIF DVHVHEVVDA SLSVIAQTFM DACTRTEHKL SRDSPSNKLL
YAKEISTYKK MVEDYYKGIR QMVQVSDQDM NTHLAEISRA HTDSLNTLVA LHQLYQYTQK
YYDEIINALE EDPAAQKMQL AFRLQQIAAA LENKVTDL
