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Database: UniProt
Entry: F6R0F1_CALJA
LinkDB: F6R0F1_CALJA
Original site: F6R0F1_CALJA 
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}.
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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
//
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