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NELL2_BOVIN
ID   NELL2_BOVIN             Reviewed;         816 AA.
AC   A6QR11;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Protein kinase C-binding protein NELL2;
DE   AltName: Full=NEL-like protein 2;
DE   Flags: Precursor;
GN   Name=NELL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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}.
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DR   EMBL; BC150070; AAI50071.1; -; mRNA.
DR   RefSeq; NP_001095554.1; NM_001102084.1.
DR   RefSeq; XP_005206438.1; XM_005206381.3.
DR   RefSeq; XP_005206439.1; XM_005206382.3.
DR   AlphaFoldDB; A6QR11; -.
DR   SMR; A6QR11; -.
DR   STRING; 9913.ENSBTAP00000042993; -.
DR   PaxDb; A6QR11; -.
DR   Ensembl; ENSBTAT00000045616; ENSBTAP00000042993; ENSBTAG00000032183.
DR   GeneID; 524622; -.
DR   KEGG; bta:524622; -.
DR   CTD; 4753; -.
DR   VEuPathDB; HostDB:ENSBTAG00000032183; -.
DR   VGNC; VGNC:32003; NELL2.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00810000125439; -.
DR   HOGENOM; CLU_006887_0_0_1; -.
DR   InParanoid; A6QR11; -.
DR   OMA; RANCVNL; -.
DR   OrthoDB; 767046at2759; -.
DR   TreeFam; TF323325; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000032183; Expressed in Ammon's horn and 82 other tissues.
DR   ExpressionAtlas; A6QR11; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
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   Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW   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_0000354681"
FT   DOMAIN          30..258
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"
SQ   SEQUENCE   816 AA;  91270 MW;  AA3407C610A18819 CRC64;
     MESRVLLRTF CLLFGLGAVW GLGVDPSLQI DVLTELELGE STTGVRQVPG LHNGTKAFLF
     QDTPRSIKAS TATAEQFFQK LRNKHEFTIL VTLKQTHLNS GVILSIHHLD HRYLELESSG
     HRNEVRLHYR SGSHHPHTEV FPYILADDKW HKLSLAISAS HLILHIDCNK IYERVVEKPS
     TDLPLGTSFW LGQRNNAHGY FKGIMQDVQL LVMPQGFIAQ CPDLNRTCPT CNDFHGLVQK
     IMELQDILAK TSAKLSRAEQ RMNRLDQCYC ERTCTMKGTT YREFESWTDG CKNCTCLNGT
     IQCETLICPN PDCPLKSAPA YVDGKCCKEC KSICQFQGRT YFEGQRNTVY SSSGVCVLYE
     CKDQSMKLVE SSGCPALDCA ESHQITLSHS CCKVCKGYDF CSERHNCMEN SVCRNLNDRA
     VCSCRDGFRA LREDNAYCED IDECAEGRHY CRENTMCVNT PGSFMCICKT GYIRIDDYSC
     TEHDECVTNQ HNCDENALCF NTVGGHNCVC KPGYTGNGTT CKAFCQDGCR NGGACIAANV
     CACPQGFTGH SCETDIDECS DGFVQCDSRA NCINLPGWYH CECRDGYHDN GMFSPSGESC
     EDIDECGTGR HSCANDTICF NLDGGYDCRC PHGKNCTGDC IHDGKIKHNG QIWVLENDRC
     SVCSCQNGFV MCRRMVCDCE NPTVDLFCCP ECDPRLSSQC LHQNGETLYN SGDTWVQNCQ
     QCRCLQGEVD CWPLPCPEVE CEFSVLPENE CCPRCVTDPC QADTIRNDIT KTCLDEMNVV
     RFTGSSWIKH GTECTLCQCK NGHICCSVDP QCLQEL
 
 
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