ID PTPRZ_RAT Reviewed; 2316 AA.
AC Q62656; Q62621;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 183.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase zeta;
DE Short=R-PTP-zeta;
DE EC=3.1.3.48 {ECO:0000269|PubMed:16814777};
DE AltName: Full=3F8 chondroitin sulfate proteoglycan;
DE AltName: Full=3H1 keratan sulfate proteoglycan;
DE AltName: Full=Phosphacan;
DE Flags: Precursor;
GN Name=Ptprz1; Synonyms=Ptprz, Ptpz;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7579589; DOI=10.3109/10425179509030989;
RA Maurel P., Meyer-Puttlitz B., Flad M., Margolis R.U., Margolis R.K.;
RT "Nucleotide sequence and molecular variants of rat receptor-type protein
RT tyrosine phosphatase-zeta/beta.";
RL DNA Seq. 5:323-328(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7511813; DOI=10.1073/pnas.91.7.2512;
RA Maurel P., Rauch U., Flad M., Margolis R.K., Margolis R.U.;
RT "Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts
RT with neurons and neural cell-adhesion molecules, is an extracellular
RT variant of a receptor-type protein tyrosine phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2512-2516(1994).
RN [3]
RP INTERACTION WITH N-CAM AND NG-CAM.
RX PubMed=7528221; DOI=10.1083/jcb.127.6.1703;
RA Milev P., Friedlander D.R., Sakurai T., Karthikeyan L., Flad M.,
RA Margolis R.K., Grumet M., Margolis R.U.;
RT "Interactions of the chondroitin sulfate proteoglycan phosphacan, the
RT extracellular domain of a receptor-type protein tyrosine phosphatase, with
RT neurons, glia, and neural cell adhesion molecules.";
RL J. Cell Biol. 127:1703-1715(1994).
RN [4]
RP INTERACTION WITH TENASCIN.
RX PubMed=7512960; DOI=10.1016/s0021-9258(17)32692-3;
RA Grumet M., Milev P., Sakurai T., Karthikeyan L., Bourdon M., Margolis R.K.,
RA Margolis R.U.;
RT "Interactions with tenascin and differential effects on cell adhesion of
RT neurocan and phosphacan, two major chondroitin sulfate proteoglycans of
RT nervous tissue.";
RL J. Biol. Chem. 269:12142-12146(1994).
RN [5]
RP INTERACTION WITH CONTACTIN.
RX PubMed=7628014; DOI=10.1016/0092-8674(95)90312-7;
RA Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S.,
RA Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M.,
RA Schlessinger J.;
RT "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a
RT functional ligand for the axonal cell recognition molecule contactin.";
RL Cell 82:251-260(1995).
RN [6]
RP INTERACTION WITH MDK.
RX PubMed=10212223; DOI=10.1074/jbc.274.18.12474;
RA Maeda N., Ichihara-Tanaka K., Kimura T., Kadomatsu K., Muramatsu T.,
RA Noda M.;
RT "A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a
RT heparin-binding growth factor midkine. Involvement of arginine 78 of
RT midkine in the high affinity binding to PTPzeta.";
RL J. Biol. Chem. 274:12474-12479(1999).
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH
RP PTN.
RX PubMed=16814777; DOI=10.1016/j.febslet.2006.06.041;
RA Fukada M., Fujikawa A., Chow J.P., Ikematsu S., Sakuma S., Noda M.;
RT "Protein tyrosine phosphatase receptor type Z is inactivated by ligand-
RT induced oligomerization.";
RL FEBS Lett. 580:4051-4056(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572; SER-576; SER-645;
RP SER-647 AND THR-1688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protein tyrosine phosphatase that negatively regulates
CC oligodendrocyte precursor proliferation in the embryonic spinal cord.
CC Required for normal differentiation of the precursor cells into mature,
CC fully myelinating oligodendrocytes. May play a role in protecting
CC oligondendrocytes against apoptosis. May play a role in the
CC establishment of contextual memory, probably via the dephosphorylation
CC of proteins that are part of important signaling cascades (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform 3 (phosphacan), previously designated 3F8 chondroitin
CC sulfate proteoglycan or 3H1 keratan sulfate proteoglycan depending on
CC the glycosylation status, is a soluble nervous tissue-specific
CC proteoglycan. It is synthesized by glia and binds to neurons and to the
CC neural cell adhesion molecules tenascin, N-CAM or NG-CAM but not to
CC laminin and fibronectin. Phosphacan acts as a potent inhibitor of cell
CC adhesion and neurite outgrowth.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:16814777};
CC -!- SUBUNIT: Interacts with tenascin (PubMed:7512960). Interacts with N-CAM
CC and NG-CAM (PubMed:7528221). The carbonic-anhydrase like domain
CC interacts with CNTN1 (contactin) (PubMed:7628014). Interacts with PTN
CC (PubMed:16814777). Interaction with PTN promotes formation of
CC homooligomers; oligomerization impairs phosphatase activity
CC (PubMed:16814777). Interacts (via chondroitin sulfate chains) with MDK
CC (via C-terminal); this interaction is inhibited by PTN; this
CC interaction promotes neuronal migration (PubMed:10212223).
CC {ECO:0000269|PubMed:10212223, ECO:0000269|PubMed:16814777,
CC ECO:0000269|PubMed:7512960, ECO:0000269|PubMed:7528221,
CC ECO:0000269|PubMed:7628014}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:16814777}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16814777}. Secreted {ECO:0000250}. Note=A secreted
CC form is apparently generated by shedding of the extracellular domain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q62656-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q62656-2; Sequence=VSP_005152;
CC Name=3; Synonyms=Phosphacan;
CC IsoId=Q62656-3; Sequence=VSP_005153, VSP_005154;
CC -!- TISSUE SPECIFICITY: Nervous tissue specific.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000305}.
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DR EMBL; U09357; AAC52207.1; -; mRNA.
DR EMBL; U04998; AAC52383.1; -; mRNA.
DR PIR; A40169; A40169.
DR RefSeq; NP_001164156.1; NM_001170685.1.
DR RefSeq; NP_037212.2; NM_013080.2.
DR PDB; 6J6U; X-ray; 3.32 A; A/B=1699-2316.
DR PDBsum; 6J6U; -.
DR AlphaFoldDB; Q62656; -.
DR SMR; Q62656; -.
DR BioGRID; 247642; 12.
DR DIP; DIP-59715N; -.
DR IntAct; Q62656; 1.
DR STRING; 10116.ENSRNOP00000008719; -.
DR GlyCosmos; Q62656; 22 sites, No reported glycans.
DR GlyGen; Q62656; 22 sites.
DR iPTMnet; Q62656; -.
DR PhosphoSitePlus; Q62656; -.
DR SwissPalm; Q62656; -.
DR PaxDb; 10116-ENSRNOP00000008719; -.
DR Ensembl; ENSRNOT00065040721; ENSRNOP00065033210; ENSRNOG00065023697. [Q62656-1]
DR GeneID; 25613; -.
DR KEGG; rno:25613; -.
DR UCSC; RGD:3455; rat. [Q62656-1]
DR AGR; RGD:3455; -.
DR CTD; 5803; -.
DR RGD; 3455; Ptprz1.
DR eggNOG; KOG0789; Eukaryota.
DR InParanoid; Q62656; -.
DR OrthoDB; 2903434at2759; -.
DR PhylomeDB; Q62656; -.
DR Reactome; R-RNO-201556; Signaling by ALK.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR PRO; PR:Q62656; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0072534; C:perineuronal net; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; IPI:RGD.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; IDA:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:RGD.
DR GO; GO:2000171; P:negative regulation of dendrite development; IDA:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR GO; GO:1900006; P:positive regulation of dendrite development; IDA:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:RGD.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; IMP:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
DR GO; GO:0008542; P:visual learning; IEP:RGD.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd17669; R-PTP-Z-2; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT CHAIN 25..2316
FT /note="Receptor-type tyrosine-protein phosphatase zeta"
FT /id="PRO_0000025469"
FT TOPO_DOM 25..1637
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1638..1663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1664..2316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..300
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 314..413
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1718..1993
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 2024..2283
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 433..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1934
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1902
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1934..1940
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1978
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 2224
FT /note="Ancestral active site"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 645
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1685
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:B9EKR1"
FT MOD_RES 1688
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2056
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23471"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1005
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1058
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1550
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1552
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..240
FT /evidence="ECO:0000250"
FT DISULFID 133..264
FT /evidence="ECO:0000250"
FT VAR_SEQ 763..1615
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7579589"
FT /id="VSP_005152"
FT VAR_SEQ 1616
FT /note="E -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7511813"
FT /id="VSP_005153"
FT VAR_SEQ 1617..2316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7511813"
FT /id="VSP_005154"
FT TURN 1702..1704
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1705..1714
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1717..1725
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1745..1747
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1756..1759
FT /evidence="ECO:0007829|PDB:6J6U"
FT TURN 1764..1766
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1767..1769
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1783..1791
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1794..1801
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1809..1818
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1823..1826
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1830..1832
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1844..1850
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1853..1862
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1864..1876
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1890..1897
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1902..1904
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1910..1923
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1930..1933
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1935..1938
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1939..1956
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 1958..1960
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1962..1972
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 1980..1996
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2001..2003
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2006..2012
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2023..2031
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2050..2052
FT /evidence="ECO:0007829|PDB:6J6U"
FT TURN 2062..2064
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2065..2067
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2078..2084
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2092..2096
FT /evidence="ECO:0007829|PDB:6J6U"
FT TURN 2101..2103
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2104..2114
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2118..2121
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2143..2145
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2148..2152
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2156..2159
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2165..2179
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2181..2188
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2191..2193
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2195..2197
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2199..2201
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2202..2215
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2220..2223
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2225..2228
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2229..2247
FT /evidence="ECO:0007829|PDB:6J6U"
FT STRAND 2248..2250
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2252..2262
FT /evidence="ECO:0007829|PDB:6J6U"
FT HELIX 2270..2283
FT /evidence="ECO:0007829|PDB:6J6U"
SQ SEQUENCE 2316 AA; 255342 MW; 419EA9B89BDD165F CRC64;
MRILQSFLAC VQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK
QSPINIDEDL TQVNVNLKKL KFQGWEKPSL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV
FKASKMTFHW GKCNVSSEGS EHSLEGQKFP LEMQIYCFDA DRFSSFEETV KGKGRLRALS
ILFEIGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFILQNL LPNSTDKYYI YNGSLTSPPC
TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
TGKEEIHEAV CSSEPENVQA DPENYTSLLI TWERPRVVYD TMIEKFAVLY QPLEGNDQTK
HEFLTDGYQD LGAILNNLIP NMSYVLQIVA ICSNGLYGKY SDQLIVDMPT EDAELDLFPE
LIGTEEIIKE ENYGKGNEED TGLNPGRDSA TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN
RSPTRGSEFS GKSDVLNTSL NPTSQQVAEF NPEREMSLPS QIGTNLPPHS VEGTSASLNS
GSKTLLVFPQ MNLSGTAESL NMVSITEYKE VSADLSEEEN LLTDFKLDSG ADDSSGSSPA
SSTVPFSTDN LSHGYTSSSD TPEAVTYDVL RPESTRNALE DSAPSGSEES LKDPSLEGSV
WFPGSTDLTT QSETGSGREG FLQVNSTDFQ VDESRETTET FSPDATASRG PSVTDMEMPH
YSTFAYPPTE VTSHAFTPSS RPLDLAPTSN ILHSQTTQPV YNGETPLQPS YSSEVFPLVT
PLLLDNQTLN TTPAASSSDS ALHATPVFPS VGVSFDSILS SYDDAPLLPF SSASFSSDLF
HHLHTVSQTL PQVTSAAERD ELSLHASLLV AGGDLLLEPS LVQYSDVMSH QVTIHAASDT
LEFGSESAVL YKTSMVSQIE SPSSDVVMHA YSSGPETSYA IEGSHHVLTV SSSSAIPVHD
SVGVADQGSL LINPSHISLP ESSFITPTAS LLQLPPALSG DGEWSGASSD SELLLPDTDG
LRTLNMSSPV SVADFTYTTS VSGDDIKPLS KGEMMYGNET ELKMSSFSDM AYPSKSTVVP
KMSDIVNKWS ESLKETSVSV SSINSVFTES LVYPITKVFD QEISRVPEII FPVKPTHTAS
QASGDTWLKP GLSTNSEPAL SDTASSEVSH PSTQPLLYEA ASPFNTEALL QPSFPASDVD
TLLKTALPSG PRDPVLTETP MVEQSSSSVS LPLASESASS KSTLHFTSVP VLNMSPSDVH
PTSLQRLTVP HSREEYFEQG LLKSKSPQQV LPSLHSHDEF FQTAHLDISQ AYPPKGRHAF
ATPILSINEP QNTLINRLVY SEDIFMHPEI SITDKALTGL PTTVSDVLIA TDHSVPLGSG
PISMTTVSPN RDDSVTTTKL LLPSKATSKP THSARSDADL VGGGEDGDDY DDDDYDDIDS
DRFPVNKCMS CSPYRESQEK VMNDSDTQES SLVDQSDPIS HLLSENTEEE NGGTGVTRVD
KSPDKSPPPS MLPQKHNDGR EDRDIQMGSA VLPHTPGSKA WAVLTSDEES GSGQGTSDSL
NDNETSTDFS FPDVNEKDAD GVLEADDTGI APGSPRSSTP SVTSGHSGVS NSSEAEASNS
SHESRIGLAE GLESEKKAVI PLVIVSALTF ICLVVLVGIL IYWRKCFQTA HFYLEDNTSP
RVISTPPTPI FPISDDIGAI PIKHFPKHVA DLHASNGFTE EFETLKEFYQ EVQSCTVDLG
ITADSSNHPD NKHKNRYVNI VAYDHSRVKL TQLAEKDGKL TDYINANYVD GYNRPKAYIA
AQGPLKSTAE DFWRMIWEHN VEVIVMITNL VEKGRRKCDQ YWPTDGSEEY GSFLVNQKNV
QVLAYYTVRN FTLRNTKIKK GSQKGRSSGR LVTQYHYTQW PDMGVPEYSL PVLAFVRKTA
QAKRHAVGPV VVHCSAGVGR TGTYIVLDSM LQQIQHEGTV NIFGFLKHIR SQRNYLVQTE
EQYVFIHDTL VEAILSKETE VPDSHIHSYV NTLLIPGPSG KTKLEKQFQL LSQSNILQSD
YSTALKQCNR EKNRTSSIIP VERSRVGISS LSGEGTDYIN ASYIMGYYQS NEFIITQHPL
LHTIKDFWRM IWDHNAQLVV MIPDGQNMAE DEFVYWPNKD EPINCESFKV TLMSEEHKCL
SNEEKLIVQD FILEATQDDY VLEVRHFQCP KWPNPDSPIS KTFELISIIK EEAANRDGPM
IVHDEHGGVT AGTFCALTTL MHQLEKENSM DVYQVAKMIN LMRPGVFTDI EQYQFLYKVV
LSLVSTRQEE NPSTSLDSNG AALPDGNIAE SLESLV
//
