NPHN_MOUSE
ID NPHN_MOUSE Reviewed; 1256 AA.
AC Q9QZS7; D2KXA7; Q811S5; Q925S5; Q9ESC6; Q9ET59; Q9JIX1;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Nephrin;
DE AltName: Full=Renal glomerulus-specific cell adhesion receptor;
DE Flags: Precursor;
GN Name=Nphs1; Synonyms=Nphn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=10504499; DOI=10.1046/j.1523-1755.1999.00719.x;
RA Holzman L.B., St John P.L., Kovari I.A., Verma R., Holthoefer H.,
RA Abrahamson D.R.;
RT "Nephrin localizes to the slit pore of the glomerular epithelial cell.";
RL Kidney Int. 56:1481-1491(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10820162; DOI=10.1681/asn.v116991;
RA Putaala H., Sainio K., Sariola H., Tryggvason K.;
RT "Primary structure of mouse and rat nephrin cDNA and structure and
RT expression of the mouse gene.";
RL J. Am. Soc. Nephrol. 11:991-1001(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-494 (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvEv, and C57BL/6J;
RX PubMed=12039968; DOI=10.1074/jbc.m204806200;
RA Hamano Y., Grunkemeyer J.A., Sudhakar A., Zeisberg M., Cosgrove D.,
RA Morello R., Lee B., Sugimoto H., Kalluri R.;
RT "Determinants of vascular permeability in the kidney glomerulus.";
RL J. Biol. Chem. 277:31154-31162(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SELF-ASSOCIATION, INTERACTION WITH
RP KIRREL2, AND TISSUE SPECIFICITY.
RX PubMed=19887377; DOI=10.1074/jbc.m109.060657;
RA Nishida K., Hoshino M., Kawaguchi Y., Murakami F.;
RT "Ptf1a directly controls expression of immunoglobulin superfamily molecules
RT Nephrin and Neph3 in the developing central nervous system.";
RL J. Biol. Chem. 285:373-380(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 2), TISSUE SPECIFICITY,
RP AND ALTERNATIVE SPLICING.
RC STRAIN=129/Sv;
RX PubMed=12538735; DOI=10.1097/01.asn.0000043081.65110.c4;
RA Beltcheva O., Kontusaari S., Fetissov S., Putaala H., Kilpelainen P.,
RA Hokfelt T., Tryggvason K.;
RT "Alternatively used promoters and distinct elements direct tissue-specific
RT expression of nephrin.";
RL J. Am. Soc. Nephrol. 14:352-358(2003).
RN [7]
RP INTERACTION WITH CD2AP.
RX PubMed=11733379; DOI=10.1016/s0002-9440(10)63080-5;
RA Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.;
RT "CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-
RT terminal domain.";
RL Am. J. Pathol. 159:2303-2308(2001).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11136707; DOI=10.1093/hmg/10.1.1;
RA Putaala H., Soininen R., Kilpelainen P., Wartiovaara J., Tryggvason K.;
RT "The murine nephrin gene is specifically expressed in kidney, brain and
RT pancreas: inactivation of the gene leads to massive proteinuria and
RT neonatal death.";
RL Hum. Mol. Genet. 10:1-8(2001).
RN [9]
RP INTERACTION WITH CD2AP AND NPHS2.
RX PubMed=11733557; DOI=10.1172/jci200112849;
RA Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W., Shaw A.S.,
RA Holzman L.B., Mundel P.;
RT "Podocin, a raft-associated component of the glomerular slit diaphragm,
RT interacts with CD2AP and nephrin.";
RL J. Clin. Invest. 108:1621-1629(2001).
RN [10]
RP INTERACTION WITH KIRREL1.
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=12424224; DOI=10.1096/fj.02-0242fje;
RA Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.;
RT "NEPH1 defines a novel family of podocin interacting proteins.";
RL FASEB J. 17:115-117(2003).
RN [11]
RP SELF-ASSOCIATION, AND INTERACTION WITH KIRREL1.
RX PubMed=12660326; DOI=10.1097/01.asn.0000057853.05686.89;
RA Gerke P., Huber T.B., Sellin L., Benzing T., Walz G.;
RT "Homodimerization and heterodimerization of the glomerular podocyte
RT proteins nephrin and NEPH1.";
RL J. Am. Soc. Nephrol. 14:918-926(2003).
RN [12]
RP INTERACTION WITH KIRREL3.
RX PubMed=15843475; DOI=10.1681/asn.2004060439;
RA Gerke P., Sellin L., Kretz O., Petraschka D., Zentgraf H., Benzing T.,
RA Walz G.;
RT "NEPH2 is located at the glomerular slit diaphragm, interacts with nephrin
RT and is cleaved from podocytes by metalloproteinases.";
RL J. Am. Soc. Nephrol. 16:1693-1702(2005).
RN [13]
RP INTERACTION WITH DDN.
RX PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT promotes apoptosis of podocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
RN [14]
RP INTERACTION WITH KIRREL3.
RX PubMed=18752272; DOI=10.1002/cne.21838;
RA Komori T., Gyobu H., Ueno H., Kitamura T., Senba E., Morikawa Y.;
RT "Expression of kin of irregular chiasm-like 3/mKirre in proprioceptive
RT neurons of the dorsal root ganglia and its interaction with nephrin in
RT muscle spindles.";
RL J. Comp. Neurol. 511:92-108(2008).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19470472; DOI=10.1073/pnas.0904398106;
RA Sohn R.L., Huang P., Kawahara G., Mitchell M., Guyon J., Kalluri R.,
RA Kunkel L.M., Gussoni E.;
RT "A role for nephrin, a renal protein, in vertebrate skeletal muscle cell
RT fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9274-9279(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Seems to play a role in the development or function of the
CC kidney glomerular filtration barrier. Regulates glomerular vascular
CC permeability. May anchor the podocyte slit diaphragm to the actin
CC cytoskeleton. Plays a role in skeletal muscle formation through
CC regulation of myoblast fusion. {ECO:0000269|PubMed:11136707,
CC ECO:0000269|PubMed:12039968, ECO:0000269|PubMed:19470472}.
CC -!- SUBUNIT: Interacts with NPHS2 and with CD2AP (via C-terminal domain).
CC Interacts with MAGI1 (via PDZ 2 and 3 domains) forming a tripartite
CC complex with IGSF5/JAM4. Forms a complex with ACTN4, CASK, IQGAP1,
CC MAGI2, SPTAN1 and SPTBN1 (By similarity). Interacts with DDN; the
CC interaction is direct. Self-associates (via the Ig-like domains). Also
CC interacts (via the Ig-like domains) with KIRREL1 and KIRREL2; the
CC interaction with KIRREL1 is dependent on KIRREL1 glycosylation.
CC Interacts with KIRREL3 (PubMed:15843475, PubMed:18752272).
CC {ECO:0000250|UniProtKB:Q9R044, ECO:0000269|PubMed:11733379,
CC ECO:0000269|PubMed:11733557, ECO:0000269|PubMed:12424224,
CC ECO:0000269|PubMed:12660326, ECO:0000269|PubMed:15843475,
CC ECO:0000269|PubMed:17537921, ECO:0000269|PubMed:18752272,
CC ECO:0000269|PubMed:19887377}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Located at podocyte slit diaphragm
CC between podocyte foot processes. {ECO:0000269|PubMed:10504499}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NephrinA;
CC IsoId=Q9QZS7-1; Sequence=Displayed;
CC Name=2; Synonyms=NephrinB;
CC IsoId=Q9QZS7-2; Sequence=VSP_040676;
CC -!- TISSUE SPECIFICITY: Expressed in kidney glomeruli. In the embryo,
CC expressed in the mesonephric kidney at 11 dpc with strong expression in
CC cranial tubules with podocyte-like structures. Expression is observed
CC in the podocytes of the developing kidney from 13 dpc. High expression
CC is also detected in the developing cerebellum, hindbrain, spinal cord,
CC retina and hypothalamus. Expressed in skeletal muscle during myoblast
CC fusion such as in the adult following acute injury and in the embryo
CC but not detected in uninjured adult skeletal muscle. Isoform 1 and
CC isoform 2 are expressed in the newborn brain and developing cerebellum.
CC Isoform 1 is the predominant isoform in adult kidney.
CC {ECO:0000269|PubMed:10820162, ECO:0000269|PubMed:11136707,
CC ECO:0000269|PubMed:12538735, ECO:0000269|PubMed:19470472,
CC ECO:0000269|PubMed:19887377}.
CC -!- PTM: Phosphorylated at Tyr-1208 by FYN, leading to the recruitment and
CC activation of phospholipase C-gamma-1/PLCG1. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Death by postnatal day 2 associated with
CC proteinuria, edema and massive glomerular vascular leak. Kidneys
CC display enlarged Bowman's spaces, dilated tubuli, effacement of
CC podocyte foot processes and an absence of the glomerular epithelial
CC slit diaphragm. Impaired skeletal muscle development characterized by
CC incomplete myoblast fusion. {ECO:0000269|PubMed:11136707,
CC ECO:0000269|PubMed:12039968, ECO:0000269|PubMed:19470472}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF168466; AAF03368.1; -; mRNA.
DR EMBL; AF172254; AAF91085.1; -; Genomic_DNA.
DR EMBL; AF172247; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172248; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172249; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172250; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172251; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172252; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172253; AAF91085.1; JOINED; Genomic_DNA.
DR EMBL; AF172256; AAF91087.1; -; mRNA.
DR EMBL; AF190638; AAG17142.1; -; Genomic_DNA.
DR EMBL; AF191090; AAK38483.1; -; mRNA.
DR EMBL; AB513652; BAI63574.1; -; mRNA.
DR EMBL; AC167970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY183460; AAO22850.1; -; Genomic_DNA.
DR CCDS; CCDS39884.1; -. [Q9QZS7-1]
DR RefSeq; NP_062332.2; NM_019459.2. [Q9QZS7-1]
DR RefSeq; XP_011248949.1; XM_011250647.1. [Q9QZS7-2]
DR AlphaFoldDB; Q9QZS7; -.
DR BioGRID; 207694; 5.
DR DIP; DIP-61265N; -.
DR IntAct; Q9QZS7; 3.
DR STRING; 10090.ENSMUSP00000006825; -.
DR GlyGen; Q9QZS7; 7 sites.
DR iPTMnet; Q9QZS7; -.
DR PhosphoSitePlus; Q9QZS7; -.
DR jPOST; Q9QZS7; -.
DR PaxDb; Q9QZS7; -.
DR PRIDE; Q9QZS7; -.
DR ProteomicsDB; 293879; -. [Q9QZS7-1]
DR ProteomicsDB; 293880; -. [Q9QZS7-2]
DR Antibodypedia; 29541; 780 antibodies from 40 providers.
DR DNASU; 54631; -.
DR Ensembl; ENSMUST00000006825; ENSMUSP00000006825; ENSMUSG00000006649. [Q9QZS7-1]
DR Ensembl; ENSMUST00000126297; ENSMUSP00000116500; ENSMUSG00000006649. [Q9QZS7-2]
DR GeneID; 54631; -.
DR KEGG; mmu:54631; -.
DR UCSC; uc009gem.1; mouse. [Q9QZS7-2]
DR UCSC; uc009gen.1; mouse. [Q9QZS7-1]
DR CTD; 4868; -.
DR MGI; MGI:1859637; Nphs1.
DR VEuPathDB; HostDB:ENSMUSG00000006649; -.
DR eggNOG; KOG3515; Eukaryota.
DR GeneTree; ENSGT00940000159510; -.
DR HOGENOM; CLU_003881_0_1_1; -.
DR InParanoid; Q9QZS7; -.
DR OMA; CEVSNIM; -.
DR OrthoDB; 269917at2759; -.
DR PhylomeDB; Q9QZS7; -.
DR TreeFam; TF327139; -.
DR Reactome; R-MMU-373753; Nephrin family interactions.
DR BioGRID-ORCS; 54631; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Nphs1; mouse.
DR PRO; PR:Q9QZS7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QZS7; protein.
DR Bgee; ENSMUSG00000006649; Expressed in renal glomerulus and 58 other tissues.
DR ExpressionAtlas; Q9QZS7; baseline and differential.
DR Genevisible; Q9QZS7; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IGI:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0007520; P:myoblast fusion; IMP:UniProtKB.
DR GO; GO:0072015; P:podocyte development; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:MGI.
DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR GO; GO:0036060; P:slit diaphragm assembly; IMP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 5.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 8.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 9.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Developmental protein;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Myogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1256
FT /note="Nephrin"
FT /id="PRO_0000015053"
FT TOPO_DOM 36..1078
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1100..1256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..144
FT /note="Ig-like C2-type 1"
FT DOMAIN 149..247
FT /note="Ig-like C2-type 2"
FT DOMAIN 256..347
FT /note="Ig-like C2-type 3"
FT DOMAIN 354..448
FT /note="Ig-like C2-type 4"
FT DOMAIN 454..554
FT /note="Ig-like C2-type 5"
FT DOMAIN 558..649
FT /note="Ig-like C2-type 6"
FT DOMAIN 754..846
FT /note="Ig-like C2-type 7"
FT DOMAIN 852..953
FT /note="Ig-like C2-type 8"
FT DOMAIN 957..1051
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 491..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60500"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R044"
FT MOD_RES 1115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R044"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R044"
FT MOD_RES 1208
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9R044"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 174..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 279..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 375..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 479..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 581..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 775..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 877..934
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..33
FT /note="MGAKEATVRGPGASPVHRTCHLIPLLLAGMLTT -> MEKWRAWDPQSIQRR
FT KTAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19887377"
FT /id="VSP_040676"
FT CONFLICT 1..24
FT /note="MGAKEATVRGPGASPVHRTCHLIP -> MALGTTLRAS (in Ref. 1;
FT AAF03368)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="A -> V (in Ref. 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="H -> R (in Ref. 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> P (in Ref. 2; AAF91085, 3; AAG17142/AAK38483
FT and 4; BAI63574)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="V -> I (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="S -> R (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> V (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> P (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="D -> G (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="T -> A (in Ref. 1; AAF03368)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="S -> T (in Ref. 1; AAF03368 and 2; AAF91087)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="L -> Q (in Ref. 1; AAF03368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1256 AA; 136336 MW; 339A670F2AF000A2 CRC64;
MGAKEATVRG PGASPVHRTC HLIPLLLAGM LTTGLAQSPV PTSAPRGFWA LSENLTVVEG
STVKLWCGVR APGSVVQWAK DGLLLGPNPK IPGFPRYSLE GDSAKGEFHL LIEACDLSDD
AEYECQVGRS ELGPELVSPS VILSILVSPK VLQLTPEAGS TVTWVAGQEY VVTCVSGDAK
PAPDIIFIQG GRTVEDVSSS VNEGSEEKLF FTEAEARVTP QSSDNGQLLV CEGSNPALAT
PIKASFTMNI LFPPGPPVID WPGLNEGHVR AGENLELPCI ARGGNPPATL QWLKNGKPVS
IAWGTEHAQA VAHSVLVMTV RPEDHGARLS CQSYNSVSAE TQERSITLQV TFPPSAVTIL
GSTSQSENKN VTLCCLTKSS RPRVLLRWWL GGRQLLPTDE TVMDGLHGGH ISMSNLTLLV
KREDNGLSLT CEAFSDAFSK ETFKKSLTLN VKYPAQKLWI EGPPEGQSIR TGTRVRLVCL
AIGGNPEPSL TWLKDSRPVN DPRQSQEPRR VQLGSVEKSG STFSRELVLI IGPPDNLAKF
SCKAGQLSAS TQLVVQFPPT NLTILANSSA LRPGDALNLT CVSISSNPPV NLSLDKEGER
LDDVAAKPQS APFKGSAASR SVFLRVSSRD HGHRVTCRAH SEALRETVSS FYRLNVLYPP
EFLGEQVRAV TVVEQGQALL PVSVSANPAP EAFNWTFRGY RLSPAGGPRH RILSGGALQL
WNVTRADDGF YQLHCQNSEG TAEALLKLDV HYAPTIRALK DPTEVNVGGS VDIVCTVDAN
PILPEMFSWE RLGEDEEELN LDDMEKMSKG STGRLRIRQA KLSQAGAYQC IVDNGVAPAA
RGLVRLVVRF APQVDHPTPL TKVAAAGDST SSATLHCRAR GVPNIDFTWT KNGVPLDLQD
PRYTEHKYHQ GVVHSSLLTI ANVSAAQDYA LFKCTATNAL GSDHTNIQLV SISRPDPPLG
LKVVSVSPHS VGLEWKPGFD GGLPQRFQIR YEALESPGFL YMDVLPAQAT TFTLTGLKPS
TRYRIWLLAS NALGDSGLTD KGIQVSITTP GLDQAPEDTD QPLPTEQPPG PPRLPLLPVL
FAVGGLLLLS NASCVGGLLW RRRLRRLAEE ISEKTEAGSE EDRIRNEYEE SQWTGDRDTR
SSTVSTAEVD PHYYSMRDFS PQLPPTLEEV SYRQAFTGIE DEDMAFPGHL YDEVERVYGP
PGVWGPLYDE VQMDPYDLRW PEVKYEDPRG IYDQVAADMD AGEPGSLPFE LRGHLV
