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SH3 and multiple ankyrin repeat domains protein 2 (Shank2) (Cortactin-binding protein 1) (CortBP1) (GKAP/SAPAP-interacting protein) (Proline-rich synapse-associated protein 1) (ProSAP1) (SPANK-3)

 SHAN2_RAT               Reviewed;        1474 AA.
Q9QX74; O70470; Q6WB19; Q9QX93; Q9QZZ9; Q9WUV9; Q9WUW0; Q9WV46;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
26-JUL-2002, sequence version 2.
22-NOV-2017, entry version 141.
RecName: Full=SH3 and multiple ankyrin repeat domains protein 2;
Short=Shank2;
AltName: Full=Cortactin-binding protein 1;
Short=CortBP1;
AltName: Full=GKAP/SAPAP-interacting protein;
AltName: Full=Proline-rich synapse-associated protein 1;
Short=ProSAP1;
AltName: Full=SPANK-3;
Name=Shank2; Synonyms=Cortbp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH CTTN.
TISSUE=Hippocampus;
PubMed=9742101; DOI=10.1128/MCB.18.10.5838;
Du Y., Weed S.A., Xiong W.-C., Marshall T.D., Parsons J.T.;
"Identification of a novel cortactin SH3 domain-binding protein and
its localization to growth cones of cultured neurons.";
Mol. Cell. Biol. 18:5838-5851(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5 AND 6), TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Brain, and Hippocampus;
PubMed=10414979;
Boeckers T.M., Kreutz M.R., Winter C., Zuschratter W., Smalla K.-H.,
Sanmarti-Vila L., Wex H., Langnaese K., Bockmann J., Garner C.C.,
Gundelfinger E.D.;
"Proline-rich synapse-associated protein-1/cortactin binding protein 1
(ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the
postsynaptic density.";
J. Neurosci. 19:6506-6518(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND TISSUE SPECIFICITY.
TISSUE=Hepatocyte;
PubMed=14977424; DOI=10.1042/BJ20031577;
McWilliams R.R., Gidey E., Fouassier L., Weed S.A., Doctor R.B.;
"Characterization of an ankyrin repeat-containing Shank2 isoform
(Shank2E) in liver epithelial cells.";
Biochem. J. 380:181-191(2004).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4/5/6), TISSUE
SPECIFICITY, AND FUNCTION.
TISSUE=Brain;
PubMed=10506216; DOI=10.1074/jbc.274.41.29510;
Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M.,
Kim E.;
"Characterization of the shank family of synaptic proteins. Multiple
genes, alternative splicing, and differential expression in brain and
development.";
J. Biol. Chem. 274:29510-29518(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-656 (ISOFORM 3).
PubMed=10958799; DOI=10.1074/jbc.M006448200;
Tobaben S., Suedhof T.C., Stahl B.;
"The G protein-coupled receptor CL1 interacts directly with proteins
of the Shank family.";
J. Biol. Chem. 275:36204-36210(2000).
[6]
INTERACTION WITH DLGAP1 AND DLG4.
PubMed=10527873; DOI=10.1006/bbrc.1999.1489;
Boeckers T.M., Winter C., Smalla K.-H., Kreutz M.R., Bockmann J.,
Seidenbecher C., Garner C.C., Gundelfinger E.D.;
"Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact
with synaptic proteins of the SAPAP/GKAP family.";
Biochem. Biophys. Res. Commun. 264:247-252(1999).
[7]
INTERACTION WITH ALPHA-LATROTOXIN RECEPTOR 1.
PubMed=10964907; DOI=10.1074/jbc.C000490200;
Kreienkamp H.-J., Zitzer H., Gundelfinger E.D., Richter D.,
Bockers T.M.;
"The calcium-independent receptor for alpha-latrotoxin from human and
rodent brains interacts with members of the ProSAP/SSTRIP/Shank family
of multidomain proteins.";
J. Biol. Chem. 275:32387-32390(2000).
[8]
REVIEW.
PubMed=10806096;
Sheng M., Kim E.;
"The Shank family of scaffold proteins.";
J. Cell Sci. 113:1851-1856(2000).
[9]
TISSUE SPECIFICITY, AND INTERACTION WITH CFTR.
PubMed=14679199; DOI=10.1074/jbc.M312871200;
Kim J.Y., Han W., Namkung W., Lee J.H., Kim K.H., Shin H., Kim E.,
Lee M.G.;
"Inhibitory regulation of cystic fibrosis transmembrane conductance
regulator anion-transporting activities by Shank2.";
J. Biol. Chem. 279:10389-10396(2004).
[10]
INTERACTION WITH DBNL.
PubMed=15014124; DOI=10.1523/JNEUROSCI.5479-03.2004;
Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D.,
Kessels M.M.;
"Linkage of the actin cytoskeleton to the postsynaptic density via
direct interactions of Abp1 with the ProSAP/Shank family.";
J. Neurosci. 24:2481-2495(2004).
[11]
INTERACTION WITH PLCB3.
PubMed=15632121; DOI=10.1074/jbc.M410740200;
Hwang J.-I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.-G.;
"The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-
mediated calcium signal.";
J. Biol. Chem. 280:12467-12473(2005).
[12]
INTERACTION WITH SLC9A3.
PubMed=16293618; DOI=10.1074/jbc.M509786200;
Han W., Kim K.H., Jo M.J., Lee J.H., Yang J., Doctor R.B., Moe O.W.,
Lee J., Kim E., Lee M.G.;
"Shank2 associates with and regulates Na+/H+ exchanger 3.";
J. Biol. Chem. 281:1461-1469(2006).
[13]
TISSUE SPECIFICITY.
PubMed=16758162; DOI=10.1007/s00418-006-0199-9;
Redecker P., Bockmann J., Boeckers T.M.;
"Expression of postsynaptic density proteins of the ProSAP/Shank
family in the thymus.";
Histochem. Cell Biol. 126:679-685(2006).
[14]
INTERACTION WITH ABI1.
PubMed=17304222; DOI=10.1038/sj.emboj.7601569;
Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J.,
Kreutz M.R., Gundelfinger E.D., Boeckers T.M.;
"Abelson interacting protein 1 (Abi-1) is essential for dendrite
morphogenesis and synapse formation.";
EMBO J. 26:1397-1409(2007).
[15]
INTERACTION WITH PDE4D, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17244609; DOI=10.1074/jbc.M610857200;
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M.,
Lee M.G.;
"Dynamic regulation of cystic fibrosis transmembrane conductance
regulator by competitive interactions of molecular adaptors.";
J. Biol. Chem. 282:10414-10422(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-648 AND
SER-1338, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373 (ISOFORMS
2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 (ISOFORMS
4; 5 AND 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Seems to be an adapter protein in the postsynaptic
density (PSD) of excitatory synapses that interconnects receptors
of the postsynaptic membrane including NMDA-type and metabotropic
glutamate receptors, and the actin-based cytoskeleton. May play a
role in the structural and functional organization of the
dendritic spine and synaptic junction.
{ECO:0000269|PubMed:10506216}.
-!- SUBUNIT: Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP.
Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-
latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2,
SLC9A3, PLCB3 and CFTR. Interacts with ABI1 (via SH3 domain).
Interacts (via proline-rich region) with PDE4D isoform 5 (via N-
terminal region). Interacts with PDE4D isoform 33, isoform 4,
isoform 7, isoform 8 and isoform 9 but not isoform 32 and isoform
6. Interacts weakly with PDE4D isoform 31. Interacts with ABI1.
{ECO:0000269|PubMed:10527873, ECO:0000269|PubMed:10964907,
ECO:0000269|PubMed:14679199, ECO:0000269|PubMed:15014124,
ECO:0000269|PubMed:15632121, ECO:0000269|PubMed:16293618,
ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:17304222,
ECO:0000269|PubMed:9742101}.
-!- INTERACTION:
Q9ES28-2:Arhgef7 (xeno); NbExp=4; IntAct=EBI-397902, EBI-8620514;
P13569:CFTR (xeno); NbExp=2; IntAct=EBI-397902, EBI-349854;
P14270-8:Pde4d; NbExp=4; IntAct=EBI-397902, EBI-9032440;
P26433:Slc9a3; NbExp=2; IntAct=EBI-397902, EBI-961694;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:17244609}. Cytoplasm
{ECO:0000269|PubMed:17244609}. Cell junction, synapse
{ECO:0000269|PubMed:17244609}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:17244609}. Cell projection, growth cone
{ECO:0000269|PubMed:17244609}. Cell projection, dendritic spine
{ECO:0000250}. Note=Colocalizes with cortactin in growth cones in
differentiating hippocampal neurons. Present in the dendritic
spines of cerebellar Purkinje cells (By similarity). Colocalizes
with cortactin in growth cones in differentiating hippocampal
neurons. Colocalized with PDE4D to the apical membrane of colonic
crypt cells. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=So far detected are complete isoforms 2 to 5.
Experimental confirmation may be lacking for some isoforms.;
Name=1;
IsoId=Q9QX74-1; Sequence=Displayed;
Name=2;
IsoId=Q9QX74-2; Sequence=VSP_006083;
Note=Contains a phosphoserine at position 373.
{ECO:0000244|PubMed:22673903};
Name=3;
IsoId=Q9QX74-3; Sequence=VSP_006083, VSP_006084, VSP_006086;
Note=Contains a phosphoserine at position 373.
{ECO:0000244|PubMed:22673903};
Name=4;
IsoId=Q9QX74-4; Sequence=VSP_006081, VSP_006082, VSP_006083;
Note=Contains a phosphoserine at position 162.
{ECO:0000244|PubMed:22673903};
Name=5;
IsoId=Q9QX74-5; Sequence=VSP_006081, VSP_006082, VSP_006083,
VSP_006084;
Note=Contains a phosphoserine at position 162.
{ECO:0000244|PubMed:22673903};
Name=6;
IsoId=Q9QX74-6; Sequence=VSP_006081, VSP_006082, VSP_006083,
VSP_006085;
Note=Contains a phosphoserine at position 162.
{ECO:0000244|PubMed:22673903};
Name=7; Synonyms=E;
IsoId=Q9QX74-7; Sequence=VSP_020049, VSP_020050;
Note=Contains 6 ANK repeats at positions 196-226, 230-259,
263-293, 297-326, 330-359, 363-393.;
-!- TISSUE SPECIFICITY: Expressed in epithelial cells (at protein
level). All isoforms except isoform 7 are expressed predominantly
in brain, with highest levels in olfactory bulb, cerebral cortex,
cerebellum, central gray matter and hippocampus. Moderate levels
of expression are seen in the caudate putamen, thalamic nuclei and
brain stem. In cerebellum primarily expressed in Purkinje cells.
Isoform 7 is not expressed in brain but expressed in liver,
cholangiocytes and thymus. Isoform 7 is present in pancreas,
colonic mucosa and thymocytes (at protein level).
{ECO:0000269|PubMed:10414979, ECO:0000269|PubMed:10506216,
ECO:0000269|PubMed:14679199, ECO:0000269|PubMed:14977424,
ECO:0000269|PubMed:16758162, ECO:0000269|PubMed:17244609}.
-!- DEVELOPMENTAL STAGE: Expressed during early postnatal brain
development, especially in the caudate putamen and thalamic
nuclei. Expression in the cerebral cortex, the hippocampus and the
cerebellum is moderate to high at P5 and shows a stable expression
throughout development. Isoforms 1, 2, 4 and 6 are predominantly
expressed in cerebellum up to the age of approximately 3 weeks.
Isoform 1 expression decreases during development of cortex but
slightly increases in cerebellum. {ECO:0000269|PubMed:10414979}.
-!- DOMAIN: The PDZ domain is required for interaction with GRID2,
PLCB3, SLC9A3 and CFTR.
-!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD42977.1; Type=Frameshift; Positions=46, 165; Evidence={ECO:0000305};
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EMBL; AF060116; AAC62226.1; -; mRNA.
EMBL; AJ249562; CAB56522.1; -; mRNA.
EMBL; AJ131899; CAB44314.1; -; mRNA.
EMBL; AJ131899; CAB44312.1; -; mRNA.
EMBL; AJ131899; CAB44313.1; -; mRNA.
EMBL; AY298755; AAP85236.1; -; mRNA.
EMBL; AF141903; AAF02497.1; -; mRNA.
EMBL; AF159048; AAD42977.1; ALT_FRAME; mRNA.
PIR; T14272; T14272.
RefSeq; NP_001004133.1; NM_001004133.1.
RefSeq; NP_597684.1; NM_133440.1. [Q9QX74-4]
RefSeq; NP_597685.1; NM_133441.1. [Q9QX74-2]
RefSeq; NP_958738.1; NM_201350.1. [Q9QX74-7]
RefSeq; XP_017444213.1; XM_017588724.1. [Q9QX74-7]
UniGene; Rn.14545; -.
ProteinModelPortal; Q9QX74; -.
SMR; Q9QX74; -.
BioGrid; 251104; 2.
CORUM; Q9QX74; -.
IntAct; Q9QX74; 11.
MINT; MINT-143507; -.
STRING; 10116.ENSRNOP00000067841; -.
iPTMnet; Q9QX74; -.
PhosphoSitePlus; Q9QX74; -.
PaxDb; Q9QX74; -.
PRIDE; Q9QX74; -.
Ensembl; ENSRNOT00000071741; ENSRNOP00000067841; ENSRNOG00000050206. [Q9QX74-1]
Ensembl; ENSRNOT00000075078; ENSRNOP00000065891; ENSRNOG00000050206. [Q9QX74-7]
Ensembl; ENSRNOT00000092357; ENSRNOP00000075800; ENSRNOG00000050206. [Q9QX74-5]
Ensembl; ENSRNOT00000092386; ENSRNOP00000075919; ENSRNOG00000050206. [Q9QX74-4]
Ensembl; ENSRNOT00000092516; ENSRNOP00000075839; ENSRNOG00000050206. [Q9QX74-2]
GeneID; 171093; -.
KEGG; rno:171093; -.
UCSC; RGD:628772; rat. [Q9QX74-1]
CTD; 22941; -.
RGD; 628772; Shank2.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4375; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00510000046474; -.
HOVERGEN; HBG054027; -.
InParanoid; Q9QX74; -.
KO; K15009; -.
PRO; PR:Q9QX74; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000050206; -.
ExpressionAtlas; Q9QX74; baseline and differential.
Genevisible; Q9QX74; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0060170; C:ciliary membrane; IDA:BHF-UCL.
GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005883; C:neurofilament; ISO:RGD.
GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0001917; C:photoreceptor inner segment; ISS:BHF-UCL.
GO; GO:0001750; C:photoreceptor outer segment; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
GO; GO:0035255; F:ionotropic glutamate receptor binding; ISS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
GO; GO:0098919; F:structural constituent of postsynaptic density; IC:SynGO.
GO; GO:0030534; P:adult behavior; ISS:BHF-UCL.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0035640; P:exploration behavior; ISS:BHF-UCL.
GO; GO:0007612; P:learning; ISS:BHF-UCL.
GO; GO:0060292; P:long term synaptic depression; ISS:BHF-UCL.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:BHF-UCL.
GO; GO:0099562; P:maintenance of postsynaptic density structure; IC:SynGO.
GO; GO:0007613; P:memory; ISS:BHF-UCL.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
GO; GO:0071625; P:vocalization behavior; ISS:BHF-UCL.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00595; PDZ; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF07653; SH3_2; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00454; SAM; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Glycoprotein; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; SH3 domain;
SH3-binding; Synapse.
CHAIN 1 1474 SH3 and multiple ankyrin repeat domains
protein 2.
/FTId=PRO_0000174674.
DOMAIN 148 207 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 248 342 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1411 1474 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
MOTIF 1169 1175 SH3-binding. {ECO:0000255}.
COMPBIAS 24 27 Poly-Arg.
COMPBIAS 521 529 Poly-Pro.
COMPBIAS 1203 1211 Poly-Pro.
MOD_RES 457 457 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 486 486 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80Z38}.
MOD_RES 586 586 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z38}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z38}.
MOD_RES 903 903 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80Z38}.
MOD_RES 1334 1334 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Z38}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 1292 1292 O-linked (GlcNAc) threonine.
{ECO:0000250}.
VAR_SEQ 1 211 Missing (in isoform 4, isoform 5 and
isoform 6). {ECO:0000303|PubMed:10414979,
ECO:0000303|PubMed:9742101}.
/FTId=VSP_006081.
VAR_SEQ 1 12 MKSLLNAFTKKE -> MPRSPTSSEDEMAQSFSDYSVGSES
DSSKEETIYDTIRATTEKPGGVKMEDLQGNTLVIRVVIQDL
QQTKCIRFNPDATVWVAKQRILCTLNQGLKDVLNYGLFQPA
SNGRDGKFLDEERLLREYPQPMGQGVPSLEFRYKKRVYKQS
NLDEKQLARLHTKTNLKKFMDHTQHRSVEKLVKLLDRGLDP
NFHDLETGETPLTLAAQLDGSMEVIKALRNGGAHLDFRSRD
GMTALHKAARMRNQVALKTLLELGASPDYKDSYGLTPLYHT
AIVGGDPYCCELLLHEHASVCCKDENGWHEIHQACRYGHVQ
HLEHLLFYGADMSAQNASGNTALHICALYNQDSCARVLLFR
GGDKELKNYNSQTPFQVAIIAGNFELAEYIKNHKETDI
(in isoform 7).
{ECO:0000303|PubMed:14977424}.
/FTId=VSP_020049.
VAR_SEQ 212 239 SQAETRADRSKKLFRHYTVGSYDSFDAA -> MMSVPGGGA
ATVMMTGYNNGRYPRNSLY (in isoform 4,
isoform 5 and isoform 6).
{ECO:0000303|PubMed:10414979,
ECO:0000303|PubMed:9742101}.
/FTId=VSP_006082.
VAR_SEQ 382 395 Missing (in isoform 7).
{ECO:0000303|PubMed:14977424}.
/FTId=VSP_020050.
VAR_SEQ 382 385 Missing (in isoform 2, isoform 3, isoform
4, isoform 5 and isoform 6).
{ECO:0000303|PubMed:10414979,
ECO:0000303|PubMed:10958799,
ECO:0000303|PubMed:9742101}.
/FTId=VSP_006083.
VAR_SEQ 388 394 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:10414979,
ECO:0000303|PubMed:10958799,
ECO:0000303|PubMed:9742101}.
/FTId=VSP_006084.
VAR_SEQ 468 483 Missing (in isoform 3).
{ECO:0000303|PubMed:10958799}.
/FTId=VSP_006086.
VAR_SEQ 468 476 Missing (in isoform 6).
{ECO:0000303|PubMed:10414979}.
/FTId=VSP_006085.
CONFLICT 35 41 PRVLLRS -> QKNLGAA (in Ref. 4).
{ECO:0000305}.
CONFLICT 152 152 L -> F (in Ref. 3; AAF02497).
{ECO:0000305}.
CONFLICT 369 369 L -> V (in Ref. 1; AAC62226).
{ECO:0000305}.
SEQUENCE 1474 AA; 158684 MW; F503D44D0D9AB7C1 CRC64;
MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA
TSHRSLSPQL LQQTPSKPDG ATKSLGSYAP GPRSRSPSLN RLGGAGEDGK RPQPPHWHVG
SPFTPGANKD SLSTFEYPGP RRKLYSAVPG RLFVAIKPYQ PQVDGEIPLH RGDRVKVLSI
GEGGFWEGSA RGHIGWFPAE CVEEVQCKPR DSQAETRADR SKKLFRHYTV GSYDSFDAAS
DCIIEDKTVV LQKKDNEGFG FVLRGAKADT PIEEFTPTPA FPALQYLESV DEGGVAWQAG
LRTGDFLIEV NNENVVKVGH RQVVNMIRQG GNHLVLKVVT VTRNLDPDDT ARKKAPPPPK
RAPTTALTLR SKSMTAELEE LGLSLVDKAS VRKKKDKPEE IVPASKPSRT AENVAIESRV
ATIKQRPTSR CFPAASDVNS VYERQGIAVM TPTVPGSPKG PFLGLPRGTM RRQKSIDSRI
FLSGITEEER QFLAPPMLKF TRSLSMPDTS EDIPPPPQSV PPSPPPPSPT TYNCPRSPTP
RVYGTIKPAF NQNPVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGMLV KQSNVEDSPE KTCSIPIPTI
IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA
RRNSPAFLST DLGDEDVGLG PPAPRMQPSK FPEEGGFGDE DETEQPLLPT PGAAPRELEN
HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAALKSSSP ASPENYVHPL TGRLLDPSSP
LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR
QETENKYETD LSKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDIPVAG PPLEEEEDRE
DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAAAPGRTI VAAGSVEEAV ILPFRIPPPP
LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKSDT PQPPSLNSSQ
PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS
ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVTEVKSPI LSGPKANVIS ELNSILQQMN
RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP
DYESRTSGPR RAPSPVVSPT ELSKEILPTP PSAAAASPSP TLSDVFSLPS QSPAGDLFGL
NPAGRSRSPS PSILQQPISN KPFTTKPVHL WTKPDVADWL ESLNLGEHKE TFMDNEIDGS
HLPNLQKEDL IDLGVTRVGH RMNIERALKQ LLDR


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