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WNT7B_CHICK
ID   WNT7B_CHICK             Reviewed;         349 AA.
AC   Q3L254; Q3L253;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein Wnt-7b;
DE   Flags: Precursor;
GN   Name=WNT7B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=16258938; DOI=10.1002/dvdy.20621;
RA   Fokina V.M., Frolova E.I.;
RT   "Expression patterns of Wnt genes during development of an anterior part of
RT   the chicken eye.";
RL   Dev. Dyn. 235:496-505(2006).
RN   [2]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND DEVELOPMENTAL STAGE.
RX   PubMed=7577679; DOI=10.1016/0925-4773(95)00385-e;
RA   Hollyday M., McMahon J.A., McMahon A.P.;
RT   "Wnt expression patterns in chick embryo nervous system.";
RL   Mech. Dev. 52:9-25(1995).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors that functions in the canonical Wnt/beta-
CC       catenin signaling pathway (By similarity). Required for normal fusion
CC       of the chorion and the allantois during placenta development (By
CC       similarity). Required for central nervous system (CNS) angiogenesis and
CC       blood-brain barrier regulation (By similarity).
CC       {ECO:0000250|UniProtKB:P28047, ECO:0000250|UniProtKB:P56706}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P56706}. Secreted
CC       {ECO:0000250|UniProtKB:P56706}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3L254-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3L254-2; Sequence=VSP_038847;
CC   -!- TISSUE SPECIFICITY: Expressed in differentiating lens fiber cells.
CC       {ECO:0000269|PubMed:16258938}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the anterior parencephalon and
CC       secondary prosencephalon at stages 20 and 24. Expressed in the
CC       ventricular epithelium of the spinal cord at the latest stages.
CC       {ECO:0000269|PubMed:7577679}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC       inhibition. {ECO:0000250|UniProtKB:P27467,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; AY753290; AAW81992.1; -; mRNA.
DR   EMBL; AY753291; AAW81993.1; -; mRNA.
DR   RefSeq; NP_001032351.1; NM_001037274.1. [Q3L254-1]
DR   RefSeq; NP_001165064.1; NM_001171593.1. [Q3L254-2]
DR   AlphaFoldDB; Q3L254; -.
DR   SMR; Q3L254; -.
DR   STRING; 9031.ENSGALP00000041983; -.
DR   PaxDb; Q3L254; -.
DR   PRIDE; Q3L254; -.
DR   Ensembl; ENSGALT00000048993; ENSGALP00000046960; ENSGALG00000036255. [Q3L254-2]
DR   Ensembl; ENSGALT00000050637; ENSGALP00000048489; ENSGALG00000036255. [Q3L254-1]
DR   GeneID; 427937; -.
DR   KEGG; gga:427937; -.
DR   CTD; 7477; -.
DR   VEuPathDB; HostDB:geneid_427937; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000158861; -.
DR   InParanoid; Q3L254; -.
DR   OMA; VHCETCT; -.
DR   OrthoDB; 745245at2759; -.
DR   PhylomeDB; Q3L254; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-GGA-3238698; WNT ligand biogenesis and trafficking.
DR   PRO; PR:Q3L254; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000036255; Expressed in cerebellum and 1 other tissue.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0070307; P:lens fiber cell development; IEP:BHF-UCL.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013300; Wnt7.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW   Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..349
FT                   /note="Protein Wnt-7b"
FT                   /id="PRO_0000392674"
FT   REGION          238..266
FT                   /note="Disordered linker"
FT                   /evidence="ECO:0000250|UniProtKB:P56706"
FT   LIPID           206
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        73..84
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        123..131
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        133..152
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        200..214
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        202..209
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        278..309
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        294..304
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        308..348
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        324..339
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        326..336
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        331..332
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   VAR_SEQ         1..24
FT                   /note="MHRNFRKWIFYVFLCFGVIYVKLG -> MILFSSRSVLLSVYYPQIFLILTS
FT                   GSYL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16258938"
FT                   /id="VSP_038847"
SQ   SEQUENCE   349 AA;  39530 MW;  7E65DDBB1F069B83 CRC64;
     MHRNFRKWIF YVFLCFGVIY VKLGALSSVV ALGANIICNK IPGLAPRQRA ICQSRPDAII
     VIGEGAQMGI NECQYQFRYG RWNCSALGEK TVFGQELRVG SREAAFTYAI TAAGVAHAVT
     AACSQGNLSN CGCDREKQGY YNQEEGWKWG GCSADIRYGI EFSRRFVDAR EIKKNARRLM
     NLHNNEAGRK VLEERMKLEC KCHGVSGSCT TKTCWTTLPK FREIGYILKE KYNAAVQVEV
     VRASRLRQPT FLKIKQIKSY QKPMETDLVY IEKSPNYCEE DASTGSVGTQ GRLCNRTSPN
     ADGCDMMCCG RGYNTHQYTK VWQCNCKFHW CCFVKCNTCS ERTEVFTCK
 
 
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