ID F6R0F1_CALJA Unreviewed; 662 AA.
AC F6R0F1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=EGF like domain multiple 6 {ECO:0000313|Ensembl:ENSCJAP00000007183.4};
GN Name=EGFL6 {ECO:0000313|Ensembl:ENSCJAP00000007183.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000007183.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000007183.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000007183.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the nephronectin family.
CC {ECO:0000256|ARBA:ARBA00009738}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F6R0F1; -.
DR STRING; 9483.ENSCJAP00000007183; -.
DR Ensembl; ENSCJAT00000007590.5; ENSCJAP00000007183.4; ENSCJAG00000003944.5.
DR GeneTree; ENSGT00930000150973; -.
DR InParanoid; F6R0F1; -.
DR OMA; NGRACID; -.
DR OrthoDB; 19806at2759; -.
DR Proteomes; UP000008225; Chromosome X.
DR Bgee; ENSCJAG00000003944; Expressed in testis.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR PANTHER; PTHR24050:SF24; EPIDERMAL GROWTH FACTOR-LIKE PROTEIN 6; 1.
DR PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 201..240
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 281..319
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 326..366
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 509..655
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 33..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72898 MW; 8F3A7811E2095C53 CRC64;
MRGSCWRRVP ARCARPAPPS LAYPVQLHPQ RSLDQACQGA LSPSRGRERP RRGARPPLSL
QRQHPVTASA AETPSGRGER RRPLSCDGVR PAPSRGGAGG GGRTPAKMPL PWGLALPLLL
PWVAGGFGNP ASARDHGLLT STHQPGVCHY GTRLACCYGW RRNSKGVCEA TCEPGCKFGE
CVGPNKCRCF PGYTGKTCSQ DMNECGMNPR PCQHRCVNTH GSYKCFCLSG HMLMPDATCV
NSRTCAMTNC QYGCEDTEEG PQCLCPSSGL RLAPDGRVCL DIDECASGKA ICPYNRRCVN
TFGSYYCKCQ VGFKLQYISG RYDCVDINEC TMDSHTCSHH ANCFNTQGSF KCKCKQGYKG
NGFRCSAIPE NSGQEVLRAP GTIKDRIKKL FAHKSSMKKK VQIKNVTPEP TRTPTHKANL
QPFNHEESIS RGGNSHGDKK GNEERMKEGF AEKKREEKAL KNDIEQERSL RGDVFSPKVN
EAGEFGLVLL QRKALTSKLE HKADLNVTVD CSFDHGICDW KQDREDDFDW NPADRDNAIG
YYMAVPALAG HKKDIGRLKL LLPDLQPQSN FCLLFDYRLA GDKVGKLRVF VKNSNNVLAW
EETTSKDGKW KTGEIQLYQG TDATKSIIFE AERGKGKISE IAVDGVLLVS GLCPDSLLSV
ED
//