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Database: UniProt
Entry: A0A2K5N9G1_CERAT
LinkDB: A0A2K5N9G1_CERAT
Original site: A0A2K5N9G1_CERAT 
ID   A0A2K5N9G1_CERAT        Unreviewed;       926 AA.
AC   A0A2K5N9G1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN   Name=NRP1 {ECO:0000313|Ensembl:ENSCATP00000034127};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000034127, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000034127, ECO:0000313|Proteomes:UP000233060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y., Hughes D.S., Murali S., Raveendran M., Korchina V., Wang M.,
RA   Jhangiani S., Bandaranaike D., Bellair M., Blankenburg K., Chao H.,
RA   Dahdouli M., Dinh H., Doddapaneni H., English A., Firestine M.,
RA   Gross S., Hernandez B., Javaid M., Jayaseelan J., Jones J., Joshi V.,
RA   Khan Z., Kovar C., Lee S., Newsham I., Nguyen L., Okwuonu G.,
RA   Ongeri F., Osuji N., Pu L.-L., Puazo M., Qu C., Quiroz J., Raj R.,
RA   Reid J.G., Santibanez J., Scheel M., Sexton D., Shah N., Skinner E.,
RA   Vee V., Wu Y., Han Y., Muzny D.M., Richards S., Worley K.C.,
RA   Rogers J., Gibbs R.A.;
RT   "Sooty reference genome and diversity panel.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCATP00000034127}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the neuropilin family.
CC       {ECO:0000256|PIRNR:PIRNR036960}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   RefSeq; XP_011940183.1; XM_012084793.1.
DR   RefSeq; XP_011940184.1; XM_012084794.1.
DR   Ensembl; ENSCATT00000058403; ENSCATP00000034127; ENSCATG00000039990.
DR   GeneID; 105597012; -.
DR   CTD; 8829; -.
DR   GeneTree; ENSGT00940000157169; -.
DR   OrthoDB; 124611at2759; -.
DR   Proteomes; UP000233060; Whole Genome Shotgun Assembly.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR   GO; GO:0038085; F:vascular endothelial growth factor binding; IEA:Ensembl.
DR   GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IEA:InterPro.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0009887; P:animal organ morphogenesis; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IEA:Ensembl.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IEA:Ensembl.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00057; FA58C; 2.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.120.290; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR014648; Neuropilin.
DR   InterPro; IPR022579; Neuropilin_C.
DR   InterPro; IPR027146; NRP1.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46806:SF4; PTHR46806:SF4; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF11980; DUF3481; 1.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF00629; MAM; 1.
DR   PIRSF; PIRSF036960; Neuropilin; 1.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00231; FA58C; 2.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01285; FA58C_1; 2.
DR   PROSITE; PS01286; FA58C_2; 2.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRNR:PIRNR036960, ECO:0000256|PIRSR:PIRSR036960-
KW   1}; Complete proteome {ECO:0000313|Proteomes:UP000233060};
KW   Developmental protein {ECO:0000256|PIRNR:PIRNR036960};
KW   Differentiation {ECO:0000256|PIRNR:PIRNR036960};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR036960-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00059, ECO:0000256|SAAS:SAAS01008102};
KW   Membrane {ECO:0000256|PIRNR:PIRNR036960, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036960-1};
KW   Neurogenesis {ECO:0000256|PIRNR:PIRNR036960};
KW   Receptor {ECO:0000256|PIRNR:PIRNR036960};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    926       Neuropilin. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014335908.
FT   TRANSMEM    860    885       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       29    143       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      149    267       CUB. {ECO:0000259|PROSITE:PS01180}.
FT   DOMAIN      277    426       F5/8 type C. {ECO:0000259|PROSITE:
FT                                PS50022}.
FT   DOMAIN      433    585       F5/8 type C. {ECO:0000259|PROSITE:
FT                                PS50022}.
FT   DOMAIN      650    814       MAM. {ECO:0000259|PROSITE:PS50060}.
FT   REGION      823    848       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   METAL       197    197       Calcium. {ECO:0000256|PIRSR:PIRSR036960-
FT                                1}.
FT   METAL       211    211       Calcium. {ECO:0000256|PIRSR:PIRSR036960-
FT                                1}.
FT   METAL       252    252       Calcium. {ECO:0000256|PIRSR:PIRSR036960-
FT                                1}.
FT   DISULFID     29     56       {ECO:0000256|PIRSR:PIRSR036960-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00059}.
FT   DISULFID     84    106       {ECO:0000256|PIRSR:PIRSR036960-2}.
FT   DISULFID    149    175       {ECO:0000256|PIRSR:PIRSR036960-2}.
FT   DISULFID    208    230       {ECO:0000256|PIRSR:PIRSR036960-2}.
FT   DISULFID    277    426       {ECO:0000256|PIRSR:PIRSR036960-2}.
FT   DISULFID    433    585       {ECO:0000256|PIRSR:PIRSR036960-2}.
SQ   SEQUENCE   926 AA;  103279 MW;  BA245B742346E382 CRC64;
     MEKGLPLLCA ALALALALAP AGAFRNDKCG DTIKIESPGY LTSPGYPHSY HPSEKCEWLI
     QAPDPYQRIM INFNPHFDLE DRDCKYDYVE VFDGENENGR LWGKFCGKIA PPPVVSSGQF
     LFIKFVSDYE THGAGFSIRY EIFKRGPECS QNYTTPSGVI KSPGFPEKYP NSLECTYIVF
     APKMSEIILE FESFDLEPDS NPPGGMFCRY DRLEIWDGFP DVGPHIGRYC GQKTPGRIRS
     SSGILSMVFY TDSAIAKEGF SANYSVLQSS VSEDFKCMEA VGMESGEIHS DQITASSQYS
     TNWSAERSRL NYPENGWTPG EDSYREWIQV DLGLLRFVTA VGTQGAISKE TKKKYYVKTY
     KIDVSSNGED WITIKEGNKP VLFQGNTNPT DVVVAVFPKP LITRFVRIKP ATWETGISMR
     FEVYGCKITD YPCSGMLGMV SGLISDSQIT SSNQGDRNWM PENIRLVTSR SGWALPPAPH
     SYVNEWLQID LGEEKIVRGI IIQGGKHREN KVFMRKFKIG YSNNGSDWKM IMDDSKRKAK
     SFEGNNNYDT PELRTFPALS TRFIRIYPER ATHGGLGLRM ELLGCEVEAP TAGPTTPNGN
     PVDECDDDQA NCHSGTGDDF QLTGGTTVLA TEKPTVIDST IQSEFPTYGF NCEFGWGSHK
     TFCHWEHDNH VQLKWSVLTS KTGPIQDHTA GDGNFIYSQA DENQKGKVAR LVSPVVYSQN
     SAHCMTFWYH MSGSHVGTLR VKLRYQKPEE YDQLVWMAIG HQGDHWKEGR VLLHKSLKLY
     QVIFEGEIGK GNLGGIAVDD ISINNHISQE DCAKPADLDK KNPEIKIDET GSTPGYEGEG
     EGDKNISRKP GNVLKTLDPI LITIIAMSAL GVLLGAVCGV VLYCACWHNG MSERNLSALE
     NYNFELVDGV KLKKDKLNTQ STYSEA
//
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