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PLPR4_HUMAN
ID   PLPR4_HUMAN             Reviewed;         763 AA.
AC   Q7Z2D5; E7EPS1; O75043; Q5T9R9; Q86XQ5; Q8N3F1; Q96MP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Phospholipid phosphatase-related protein type 4 {ECO:0000305};
DE   AltName: Full=Brain-specific phosphatidic acid phosphatase-like protein 1 {ECO:0000303|Ref.7};
DE   AltName: Full=Inactive 2-lysophosphatidate phosphatase PLPPR4 {ECO:0000305|PubMed:15280885};
DE   AltName: Full=Lipid phosphate phosphatase-related protein type 4 {ECO:0000303|Ref.2};
DE   AltName: Full=Plasticity-related gene 1 protein {ECO:0000305|PubMed:12730698};
DE            Short=PRG-1 {ECO:0000303|PubMed:12730698};
GN   Name=PLPPR4 {ECO:0000312|HGNC:HGNC:23496};
GN   Synonyms=KIAA0455 {ECO:0000303|PubMed:9455484}, LPPR4 {ECO:0000303|Ref.2},
GN   PHP1 {ECO:0000303|Ref.7}, PRG1 {ECO:0000303|PubMed:12730698};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CAUTION.
RC   TISSUE=Brain;
RX   PubMed=12730698; DOI=10.1038/nn1052;
RA   Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O., Nitsch R.;
RT   "A new phospholipid phosphatase, PRG-1, is involved in axon growth and
RT   regenerative sprouting.";
RL   Nat. Neurosci. 6:572-578(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Morris A.J., Sigal Y.J., McDermott M., Sciorra V.A.;
RT   "Lipid phosphate phosphatase related proteins.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 15-763 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-763 (ISOFORM 1).
RA   Ninnemann O., Brauer A.U., Savaskan N., Nitsch R.;
RT   "A new brain specific member of the PAP-2 family.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-763 (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   CAUTION.
RX   PubMed=15280885; DOI=10.1038/nn0804-789a;
RA   McDermott M.I., Sigal Y.J., Sciorra V.A., Morris A.J.;
RT   "Is PRG-1 a new lipid phosphatase?";
RL   Nat. Neurosci. 7:789-789(2004).
RN   [10]
RP   VARIANT THR-345, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=26671989; DOI=10.15252/emmm.201505677;
RA   Vogt J., Yang J.W., Mobascher A., Cheng J., Li Y., Liu X., Baumgart J.,
RA   Thalman C., Kirischuk S., Unichenko P., Horta G., Radyushkin K., Stroh A.,
RA   Richers S., Sahragard N., Distler U., Tenzer S., Qiao L., Lieb K.,
RA   Tuescher O., Binder H., Ferreiros N., Tegeder I., Morris A.J., Gropa S.,
RA   Nuernberg P., Toliat M.R., Winterer G., Luhmann H.J., Huai J., Nitsch R.;
RT   "Molecular cause and functional impact of altered synaptic lipid signaling
RT   due to a prg-1 gene SNP.";
RL   EMBO Mol. Med. 8:25-38(2016).
CC   -!- FUNCTION: Postsynaptic density membrane protein that indirectly
CC       regulates glutamatergic synaptic transmission through lysophosphatidic
CC       acid (LPA)-mediated signaling pathways. Binds lysophosphatidic acid
CC       (LPA) and mediates its internalization into cells. Could act as
CC       receptor or a transporter of this lipid at the post-synaptic membrane
CC       (By similarity). Modulates lysophosphatidic acid (LPA) activity in
CC       neuron axonal outgrowth during development by attenuating phospholipid-
CC       induced axon collapse (By similarity). {ECO:0000250|UniProtKB:Q7TMB7,
CC       ECO:0000250|UniProtKB:Q7TME0}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic density membrane
CC       {ECO:0000269|PubMed:26671989}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7Z2D5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z2D5-2; Sequence=VSP_030950, VSP_030951;
CC       Name=3;
CC         IsoId=Q7Z2D5-3; Sequence=VSP_046784;
CC   -!- TISSUE SPECIFICITY: Expressed by glutamatergic neurons (at protein
CC       level). {ECO:0000269|PubMed:26671989}.
CC   -!- PTM: O-glycosylated. Probably at Ser-346.
CC       {ECO:0000250|UniProtKB:Q7TME0}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Originally described as a 2-lysophosphatidate/LPA phosphatase
CC       (PubMed:12730698). However, following studies suggested it does not
CC       have such activity or only a residual one (PubMed:15280885). This is
CC       further supported by the fact that the phosphatase sequence motifs as
CC       well as the His residue acting as a nucleophile in active phosphatases
CC       of the PA-phosphatase related phosphoesterase family are not conserved
CC       (PubMed:15280885). {ECO:0000269|PubMed:12730698,
CC       ECO:0000269|PubMed:15280885}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32300.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAW72991.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF541281; AAP57770.1; -; mRNA.
DR   EMBL; AY304518; AAP72155.1; -; mRNA.
DR   EMBL; AB007924; BAA32300.3; ALT_INIT; mRNA.
DR   EMBL; AK056665; BAB71245.1; -; mRNA.
DR   EMBL; AK291369; BAF84058.1; -; mRNA.
DR   EMBL; AL136147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW72991.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471097; EAW72992.1; -; Genomic_DNA.
DR   EMBL; AF357013; AAO85400.1; -; mRNA.
DR   EMBL; AL834390; CAD39052.1; -; mRNA.
DR   RefSeq; NP_001159724.1; NM_001166252.1. [Q7Z2D5-3]
DR   RefSeq; NP_055654.2; NM_014839.4.
DR   AlphaFoldDB; Q7Z2D5; -.
DR   BioGRID; 115220; 12.
DR   STRING; 9606.ENSP00000359204; -.
DR   DEPOD; PLPPR4; -.
DR   GlyGen; Q7Z2D5; 9 sites.
DR   iPTMnet; Q7Z2D5; -.
DR   PhosphoSitePlus; Q7Z2D5; -.
DR   BioMuta; PLPPR4; -.
DR   DMDM; 74750018; -.
DR   jPOST; Q7Z2D5; -.
DR   MassIVE; Q7Z2D5; -.
DR   PaxDb; Q7Z2D5; -.
DR   PeptideAtlas; Q7Z2D5; -.
DR   PRIDE; Q7Z2D5; -.
DR   ProteomicsDB; 17424; -.
DR   ProteomicsDB; 68943; -. [Q7Z2D5-1]
DR   ProteomicsDB; 68944; -. [Q7Z2D5-2]
DR   Antibodypedia; 1575; 107 antibodies from 25 providers.
DR   DNASU; 9890; -.
DR   Ensembl; ENST00000370185.9; ENSP00000359204.4; ENSG00000117600.14.
DR   Ensembl; ENST00000457765.6; ENSP00000394913.2; ENSG00000117600.14.
DR   GeneID; 9890; -.
DR   KEGG; hsa:9890; -.
DR   UCSC; uc001dse.4; human. [Q7Z2D5-1]
DR   CTD; 9890; -.
DR   DisGeNET; 9890; -.
DR   GeneCards; PLPPR4; -.
DR   HGNC; HGNC:23496; PLPPR4.
DR   HPA; ENSG00000117600; Tissue enriched (brain).
DR   MIM; 607813; gene.
DR   neXtProt; NX_Q7Z2D5; -.
DR   VEuPathDB; HostDB:ENSG00000117600; -.
DR   eggNOG; KOG3030; Eukaryota.
DR   HOGENOM; CLU_021458_8_0_1; -.
DR   InParanoid; Q7Z2D5; -.
DR   OMA; METEPGQ; -.
DR   OrthoDB; 1621899at2759; -.
DR   PhylomeDB; Q7Z2D5; -.
DR   BRENDA; 3.1.3.4; 2681.
DR   PathwayCommons; Q7Z2D5; -.
DR   Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
DR   SignaLink; Q7Z2D5; -.
DR   BioGRID-ORCS; 9890; 4 hits in 1021 CRISPR screens.
DR   ChiTaRS; PLPPR4; human.
DR   GenomeRNAi; 9890; -.
DR   Pharos; Q7Z2D5; Tbio.
DR   PRO; PR:Q7Z2D5; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q7Z2D5; protein.
DR   Bgee; ENSG00000117600; Expressed in CA1 field of hippocampus and 143 other tissues.
DR   Genevisible; Q7Z2D5; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:UniProtKB.
DR   GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:0140354; P:lipid import into cell; ISS:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   InterPro; IPR028684; PLPPR4.
DR   PANTHER; PTHR10165; PTHR10165; 1.
DR   PANTHER; PTHR10165:SF13; PTHR10165:SF13; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..763
FT                   /note="Phospholipid phosphatase-related protein type 4"
FT                   /id="PRO_0000317436"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          33..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TMB7"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TMB7"
FT   MOD_RES         606
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TME0"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         265..322
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046784"
FT   VAR_SEQ         552..577
FT                   /note="SARAKWLKAAEKTVACNRSNSQPRIM -> RVSSKAAPRTLKAARSPALAPS
FT                   AIKP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030950"
FT   VAR_SEQ         578..763
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030951"
FT   VARIANT         2
FT                   /note="Q -> K (in dbSNP:rs712896)"
FT                   /id="VAR_050618"
FT   VARIANT         32
FT                   /note="A -> V (in dbSNP:rs35285687)"
FT                   /id="VAR_050619"
FT   VARIANT         345
FT                   /note="R -> T (in dbSNP:rs138327459)"
FT                   /evidence="ECO:0000269|PubMed:26671989"
FT                   /id="VAR_085196"
FT   CONFLICT        18
FT                   /note="A -> S (in Ref. 4; BAB71245)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        718
FT                   /note="L -> R (in Ref. 8; CAD39052)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   763 AA;  82983 MW;  F0401DD5073EBE71 CRC64;
     MQRAGSSGGR GECDISGAGR LGLEEAARLS CAVHTSPGGG RRPGQAAGMS AKERPKGKVI
     KDSVTLLPCF YFVELPILAS SVVSLYFLEL TDVFKPVHSG FSCYDRSLSM PYIEPTQEAI
     PFLMLLSLAF AGPAITIMVG EGILYCCLSK RRNGVGLEPN INAGGCNFNS FLRRAVRFVG
     VHVFGLCSTA LITDIIQLST GYQAPYFLTV CKPNYTSLNV SCKENSYIVE DICSGSDLTV
     INSGRKSFPS QHATLAAFAA VYVSMYFNST LTDSSKLLKP LLVFTFIICG IICGLTRITQ
     YKNHPVDVYC GFLIGGGIAL YLGLYAVGNF LPSDESMFQH RDALRSLTDL NQDPNRLLSA
     KNGSSSDGIA HTEGILNRNH RDASSLTNLK RANADVEIIT PRSPMGKENM VTFSNTLPRA
     NTPSVEDPVR RNASIHASMD SARSKQLLTQ WKNKNESRKL SLQVIEPEPG QSPPRSIEMR
     SSSEPSRVGV NGDHHGPGNQ YLKIQPGAVP GCNNSMPGGP RVSIQSRPGS SQLVHIPEET
     QENISTSPKS SSARAKWLKA AEKTVACNRS NSQPRIMQVI AMSKQQGVLQ SSPKNTEGST
     VSCTGSIRYK TLTDHEPSGI VRVEAHPENN RPIIQIPSTE GEGSGSWKWK APEKGSLRQT
     YELNDLNRDS ESCESLKDSF GSGDRKRSNI DSNEHHHHGI TTIRVTPVEG SEIGSETLSI
     SSSRDSTLRR KGNIILIPER SNSPENTRNI FYKGTSPTRA YKD
 
 
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