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NELL2_PONAB
ID   NELL2_PONAB             Reviewed;         816 AA.
AC   Q5R3Z7; Q5R9X4; Q5RC76;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein kinase C-binding protein NELL2;
DE   AltName: Full=NEL-like protein 2;
DE   Flags: Precursor;
GN   Name=NELL2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotrimer. Binds to PKC beta-1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5R3Z7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5R3Z7-2; Sequence=VSP_035803;
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DR   EMBL; CR858404; CAH90631.1; -; mRNA.
DR   EMBL; CR859256; CAH91436.1; -; mRNA.
DR   EMBL; CR861463; CAH93519.1; -; mRNA.
DR   RefSeq; NP_001125844.1; NM_001132372.1.
DR   RefSeq; NP_001128913.1; NM_001135441.1.
DR   AlphaFoldDB; Q5R3Z7; -.
DR   SMR; Q5R3Z7; -.
DR   STRING; 9601.ENSPPYP00000005057; -.
DR   PRIDE; Q5R3Z7; -.
DR   Ensembl; ENSPPYT00000005255; ENSPPYP00000005057; ENSPPYG00000004430. [Q5R3Z7-1]
DR   Ensembl; ENSPPYT00000057282; ENSPPYP00000044211; ENSPPYG00000004430. [Q5R3Z7-2]
DR   GeneID; 100172773; -.
DR   GeneID; 100189859; -.
DR   KEGG; pon:100189859; -.
DR   CTD; 4753; -.
DR   GeneTree; ENSGT00810000125439; -.
DR   InParanoid; Q5R3Z7; -.
DR   OrthoDB; 767046at2759; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR   CDD; cd00110; LamG; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR001007; VWF_dom.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF00093; VWC; 2.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SMART; SM00214; VWC; 3.
DR   SMART; SM00215; VWC_out; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..816
FT                   /note="Protein kinase C-binding protein NELL2"
FT                   /id="PRO_0000354682"
FT   DOMAIN          64..228
FT                   /note="Laminin G-like"
FT   DOMAIN          272..331
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          397..439
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          440..481
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          482..522
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          523..553
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          555..601
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          602..637
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          638..693
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          698..756
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        615
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        635
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        401..413
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        407..422
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        424..438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        444..457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        451..466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        468..480
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        486..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        493..508
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        510..521
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        525..535
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        529..541
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        543..552
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        559..572
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        566..581
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        583..600
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        606..619
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        613..628
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        630..636
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         3..18
FT                   /note="SRVLLRTFCLIFGLGA -> TGLGAPLFKAWLLIS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_035803"
FT   CONFLICT        137
FT                   /note="H -> R (in Ref. 1; CAH91436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="M -> T (in Ref. 1; CAH91436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="N -> S (in Ref. 1; CAH91436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="N -> S (in Ref. 1; CAH93519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        545
FT                   /note="Q -> H (in Ref. 1; CAH90631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="D -> G (in Ref. 1; CAH90631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        683
FT                   /note="T -> I (in Ref. 1; CAH90631)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   816 AA;  91304 MW;  FD61E3C23C99750A CRC64;
     MESRVLLRTF CLIFGLGAVW GLGVDPSLQI DVLTELELGE STTGVRQVPG LHNGTKAFLF
     QDTPRSVKAS TATAEQFFQK LRNKHEFTIL VTLKQTHLNS GVILSIHHLD HRYLELESSG
     HRNEVRLHYR SGSHRPHTEV FPYILADDKW HKLSLAISAS HLILHIDCNK IYERVVEKPS
     TDLPLGTTFW LGQRNNAHGY FKGIMQDVQL LVMPQGFIAQ CPDLNRTCPT CNDFHGLVQK
     IMELQDILAK TSAKLSRAEQ RMNRLDQCYC ERTCTMKGTT YREFESWIDG CKNCTCLNGT
     IQCETLICPN PDCPLNSALA YVDGKCCKEC KSICQFQGRT YFEGERNTVY SSSGVCVLYE
     CKDQTMKLVE SSGCPALDCP ESHQITLSHS CCKVCKGYDF CSERHNCMEN SVCRNLNDRA
     VCSCRDGFRA LREDNAYCED IDECAEGRHY CRENTMCVNT PGSFMCICKT GYIRIDDYSC
     TEHDECITNQ HNCDENALCF NTVGGHNCVC KPGYTGNGTT CKAFCKDGCR NGGACIAANV
     CACPQGFTGP SCETDIDECS DGFVQCDSRA NCINLPGWYH CECRDGYHDN GMFSPSGESC
     EDIDECGTGR HSCANDTICF NLDGGYDCRC PHGKNCTGDC IHDGKVKHNG QIWVLENDRC
     SVCSCQNGFV MCRRMVCDCE NPTVDLFCCP ECDPRLSSQC LHQNGETLYN SGDTWVQNCQ
     QCRCLQGEVD CWPLPCPDVE CEFSILPENE CCPRCVTDPC QADTIRNDIT KTCLDEMNVV
     RFTGSSWIKH GTECTLCQCK NGHICCSVDP QCLQEL
 
 
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