ID A0A1S3GHY7_DIPOR Unreviewed; 348 AA.
AC A0A1S3GHY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Secreted frizzled-related protein 4 isoform X1 {ECO:0000313|RefSeq:XP_012888421.1};
GN Name=Sfrp4 {ECO:0000313|RefSeq:XP_012888421.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888421.1};
RN [1] {ECO:0000313|RefSeq:XP_012888421.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888421.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC family. {ECO:0000256|ARBA:ARBA00010054}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_012888421.1; XM_013032967.1.
DR AlphaFoldDB; A0A1S3GHY7; -.
DR GeneID; 105998291; -.
DR KEGG; dord:105998291; -.
DR CTD; 6424; -.
DR InParanoid; A0A1S3GHY7; -.
DR OrthoDB; 2919179at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:UniProt.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF7; SECRETED FRIZZLED-RELATED PROTEIN 4; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00063; FRI; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50189; NTR; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..348
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010230025"
FT DOMAIN 19..139
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 170..307
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 296..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 24..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 32..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 101..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 348 AA; 40161 MW; 95CBF1C65B327847 CRC64;
MRAPRLLALC LWLRLARDVR SAPCEAVRIP MCRHMPWNLT RMPNHLHHST QENAVLAIEQ
YEELVDANCS AVLRFFLCAM YAPICALEFL HDPIKPCKSV CQRARDGCEP LMKRYNHSWP
ESLACDELPL YDRGVCISPE AIVTDLPEDV KWTDITPDMM VQEKPLDADC KRMSPDRCKC
KKVKPTLATY LSKNYSYVIH AKIKAVQRSG CHEVTTVVDV KEIFKSLSPI PRTQVPLITN
SSCQCPHILP HQDVLIMCYE WRSRMMLLEN CLVEKWRDQL SKRSIQWEER LQEQQRTIQD
KKRTAGRISR SNPPKPKAKP PIPKPASPKK NIKARSAQRK MNPKKTVS
//
