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PTPRZ_RAT
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   03-AUG-2022, entry version 178.
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   GlyGen; Q62656; 22 sites.
DR   iPTMnet; Q62656; -.
DR   PhosphoSitePlus; Q62656; -.
DR   SwissPalm; Q62656; -.
DR   PaxDb; Q62656; -.
DR   PRIDE; Q62656; -.
DR   GeneID; 25613; -.
DR   KEGG; rno:25613; -.
DR   UCSC; RGD:3455; rat. [Q62656-1]
DR   CTD; 5803; -.
DR   RGD; 3455; Ptprz1.
DR   eggNOG; KOG0789; Eukaryota.
DR   InParanoid; Q62656; -.
DR   OrthoDB; 251520at2759; -.
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:0005737; C:cytoplasm; 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:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR   GO; GO:0016020; C:membrane; 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; ISO:RGD.
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:0007420; P:brain development; IEP: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:1901216; P:positive regulation of neuron death; 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:0006470; P:protein dephosphorylation; IDA: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   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.200.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 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   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; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   SUPFAM; SSF52799; SSF52799; 2.
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
 
 
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