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Database: UniProt
Entry: A0A3Q2XDX0_HAPBU
LinkDB: A0A3Q2XDX0_HAPBU
Original site: A0A3Q2XDX0_HAPBU 
ID   A0A3Q2XDX0_HAPBU        Unreviewed;      1196 AA.
AC   A0A3Q2XDX0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Nidogen 1 {ECO:0000313|Ensembl:ENSHBUP00000033585.1};
GN   Name=NID1 {ECO:0000313|Ensembl:ENSHBUP00000033585.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033585.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000033585.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_005946897.1; XM_005946835.2.
DR   AlphaFoldDB; A0A3Q2XDX0; -.
DR   STRING; 8153.ENSHBUP00000033585; -.
DR   Ensembl; ENSHBUT00000027529.1; ENSHBUP00000033585.1; ENSHBUG00000020581.1.
DR   GeneID; 102303834; -.
DR   CTD; 562690; -.
DR   GeneTree; ENSGT00940000156318; -.
DR   OMA; PGTGNQF; -.
DR   OrthoDB; 25347at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   CDD; cd00053; EGF; 2.
DR   CDD; cd00054; EGF_CA; 1.
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; 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; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 2.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01186; EGF_2; 4.
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:UP000264840};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1196
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018628512"
FT   DOMAIN          99..262
FT                   /note="NIDO"
FT                   /evidence="ECO:0000259|PROSITE:PS51220"
FT   DOMAIN          390..623
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          622..663
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          664..706
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          711..752
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          753..789
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          796..867
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REPEAT          938..980
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          981..1023
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1024..1068
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          275..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        837..844
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   1196 AA;  131515 MW;  5231327ABD04CFBF CRC64;
     MGWKEQGWIA CLSFLGFVVS VKSISRDELF PFGPSARDQL LEPGNDQTYR LDLSKPVLFY
     DGTFLSIFIN TNGFVATTEP ESELTYLGKM PPKFGMIAAL QGDLHTSDGV GKVFFREDSS
     PDILRRAAEH INRAFPEDDE INPTNAVVVT WVDVTTHGLE SRGDSGIKKR NTFQLVIASL
     ETTSYAIVLY PRDGIKFSSM LVGDTNVIMH AGFSKGLVRG FFSSIKGPYY RTTTDDEQSV
     RALAEETNSG LRGVWVYEIG TSPFFSNVAP GEVPELPTEA PPQEDVDAYE ESSAARRPLY
     PDRPVVAYPP YLQEQTEVHP VQFQPQNPEV VEVDDPIINV DVFSYNLGSC ANNRNKCSKF
     GECRDYANGY CCHCISGFYG NGIQCVAEGK PQRVNGKVHG RVFVGRSPSP VEFANIDLHS
     YIVANEGRAY VAISDLPETV GPSLEPLVSI SGVIGWAFAL EHPGFKNGFS IIGGEFTRQA
     EVTFMPGNEK LNIRQEFKGI DEHDHLIVST NLEGRVAEVP LGSTIKLDPY SEIYQYNNNL
     ITSSSTRDYV VTLPDGSRET RRYQWRETIS FNGCYHSETL RDMKPTQMLS VDHIFAIYDP
     AQRLIRFALT SKIGDINGGQ PEQNPCLTGR HGCDTNAVCK VGEGATFTCQ CAAGFSGDGR
     ACYDNDECRE DPQLCGPNAI CNNQPGTFRC ECEEGYQFGS DQRTCIKVDR PVDHCEAGTH
     TCSPHAQCSY AGGSSYVCTC LQGFTGDGRS CQDIDECQQS RCHSDAVCYN TEGSFTCQCR
     PGYSGDGFQC LPGRPKTRCE VHRESILGVS GPQGPRPPIG AYIPTCDNNG QYEPMQCHGS
     TGHCWCVDQN GQEISGTRTG PGSRPMCIDH NTGLPPVGPR PRPDVDALTP GTHLLFAQSG
     RIEHVPLGGY DMKKNDAKPV LHLPEKVIIG VAYDCVEKMV YWTEITSPSI SKANIEGGVP
     TSVISSGLES PEGIAIDHLG RTMFWTDSAK DHIEVASLDG SNRRVLINTD LVNPRAIIAD
     PSNGNLYWAD WNRKAPKIET SYMDGSNRRV LVRDNLGLPN GLTYDPHSSQ LCWADAGTHK
     MECMDPGRGS RSTVLERIQY PFGMTAFGKN IYYTDWQRDA VIAVDRYASR ESDEFQPQKR
     TRLYGIATAY AQCPAGQNYC SGNNGGCSHL CLATPNGRSC KCPDNAAQVG CVEREY
//
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