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Database: UniProt
Entry: A0A091L601_CATAU
LinkDB: A0A091L601_CATAU
Original site: A0A091L601_CATAU 
ID   A0A091L601_CATAU        Unreviewed;      1186 AA.
AC   A0A091L601;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Nidogen-1 {ECO:0000313|EMBL:KFP50678.1};
DE   Flags: Fragment;
GN   ORFNames=N323_06080 {ECO:0000313|EMBL:KFP50678.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP50678.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP50678.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP50678.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KL297617; KFP50678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091L601; -.
DR   Proteomes; UP000053745; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; IPR024731; EGF_dom.
DR   InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR46513:SF6; NIDOGEN-1; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00682; G2F; 1.
DR   SMART; SM00135; LY; 5.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51120; LDLRB; 3.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00500};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          31..194
FT                   /note="NIDO"
FT                   /evidence="ECO:0000259|PROSITE:PS51220"
FT   DOMAIN          371..608
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          609..650
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          651..693
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          698..741
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          742..780
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          786..858
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REPEAT          929..971
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          972..1014
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1015..1059
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        828..835
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP50678.1"
FT   NON_TER         1186
FT                   /evidence="ECO:0000313|EMBL:KFP50678.1"
SQ   SEQUENCE   1186 AA;  130799 MW;  D966564B2E927F10 CRC64;
     VATNGIIAVN EPSSEEKYLG QFPVSFGAIA PFMADLDTTD GRGNVYYRED SSSDVLQLAS
     DYIKRGFPET TFDPSSVVIV TWKLVAPYQA RGEDHTLEEK RNTFQAVLAS SDASSYAIFL
     YPEDSLQFYS TYSKNDDGKI PAMVGFSQAS TNYYFWEKPG SYNIIANDED SIRNLHKSSN
     AGKQGVWVFE IGSSSESIVP AKISDVLENL ESNEQDQEMT SKPFMSDYGS TEIRQQYVTS
     SIDSTEEDQH HVTYSVPQLA AEDFLTSYQV VTGTPLTESF YSHQDFPTAK APPRQFQVQQ
     FPPQQPQVID VEEFDETGIV FRYHTDVQQT CANNRHQCSV HAICKDYPNG FCCSCIAGYK
     GNGRQCVAEG SPQRVNGKVK GRIFVGNNPV PVIFENTDLH SYVVMNQGRA YTAISTIPET
     LGYSLLPLAS IGGIIGWMFA VEQQGYKNGF SVTGGEFTRQ TEVTFLGNNE KLVIKQKFSG
     IDEHGHLTIS TEMEGRIPEI PSGASVHIEP YTELYHTSSS VITSSSTREY TVTEPERDGV
     ASTYTGAYQW RQTISFDECI HDDSHHAASA TQQLSVDSVF VLYNRDEQIL RYAMSNSIGP
     ISDGSADINR NPCYTGTHNC DTNAICRPGT GNRFFCECSI GFRGDGNVCY DVDECSEQPA
     LCGSNAVCNN QPGTYLCECV EGYQFAADGQ TCVAVEYVVN HCQTGTHNCD IPQRAQCVYT
     GGTAYICTCL PGFSGDGRAC EDVDECQQGH CHPDAFCYNT PGSFSCQCKA GYRGDGFRCV
     LGEVEKTKCQ REREVALGSG GTFFPREIRD GHFIPQCDEH GNYLPTQCHS SSGYCWCVDR
     DGNEIDGTRS GPGVRPPCLS TAAPPVVIGP SVRPDTVPLP PGTHLLFAQS GKIEHVPLDG
     NSMKKNGAKA LLHIPDKVVI GVAYDCTDKM VYWTDISGPS ISRASLQGGE PTTIIKTDLG
     SPEGIAVDHL GRNIFWTDSQ LDRIEVARLD GRQRRILFDT GLVNPRAIVV DPMRGNLYWT
     DWNREAPKIE TSYMDGTNRR ILVKDDLGLP NGLTFDPYSS MLCWVDAGTK RVECMNPNQL
     GRRKIVEGIQ YPFSVTSYGK NLYYTDWRRD AVVAVDRTIS IEKDNFQPHK RSRLYGITTA
     FAQCPGGHNY CTVNNGGCTH LCLATPGGRS CRCPDNTVGV DCIERN
//
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