ID Q5CZI2_HUMAN Unreviewed; 1180 AA. AC Q5CZI2; DT 29-MAR-2005, integrated into UniProtKB/TrEMBL. DT 29-MAR-2005, sequence version 1. DT 14-DEC-2022, entry version 114. DE SubName: Full=Uncharacterized protein DKFZp686D12108 {ECO:0000313|EMBL:CAI56714.1}; DE Flags: Fragment; GN Name=DKFZp686D12108 {ECO:0000313|EMBL:CAI56714.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CAI56714.1}; RN [1] {ECO:0000313|EMBL:CAI56714.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fetal kidney {ECO:0000313|EMBL:CAI56714.1}; RG The German cDNA Consortium; RA Bloecker H., Boecher M., Brandt P., Mewes H.W., Weil B., Amid C., RA Osanger A., Fobo G., Han M., Wiemann S.; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. 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 EMBL; BX648241; CAI56714.1; -; mRNA. DR AlphaFoldDB; Q5CZI2; -. DR MaxQB; Q5CZI2; -. DR PeptideAtlas; Q5CZI2; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro. DR CDD; cd00255; nidG2; 1. DR CDD; cd00191; TY; 2. DR Gene3D; 2.40.155.10; -; 1. DR Gene3D; 4.10.800.10; -; 2. 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; IPR003886; NIDO_dom. DR InterPro; IPR000716; Thyroglobulin_1. DR InterPro; IPR036857; Thyroglobulin_1_sf. DR Pfam; PF12662; cEGF; 1. DR Pfam; PF12947; EGF_3; 1. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF07474; G2F; 1. DR Pfam; PF06119; NIDO; 1. DR Pfam; PF00086; Thyroglobulin_1; 2. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 4. DR SMART; SM00682; G2F; 1. DR SMART; SM00539; NIDO; 1. DR SMART; SM00211; TY; 2. DR SUPFAM; SSF54511; GFP-like; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 2. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS50026; EGF_3; 4. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS51220; NIDO; 1. DR PROSITE; PS50993; NIDOGEN_G2; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2. PE 2: Evidence at transcript level; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 110..275 FT /note="NIDO" FT /evidence="ECO:0000259|PROSITE:PS51220" FT DOMAIN 530..760 FT /note="Nidogen G2 beta-barrel" FT /evidence="ECO:0000259|PROSITE:PS50993" FT DOMAIN 761..802 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 803..845 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 850..893 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 894..930 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 939..1007 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000259|PROSITE:PS51162" FT DOMAIN 1018..1086 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000259|PROSITE:PS51162" FT REGION 352..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 994..1018 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 998..1016 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 976..983 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500" FT DISULFID 1056..1063 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAI56714.1" SQ SEQUENCE 1180 AA; 129673 MW; 3DADEC2BFAAEDC29 CRC64; TPQTERITHS SVSWSFLLRF SRGKLLMLRA AALHPDELFP HGESWGDQLL QEGDDESSAV VKLANPLHFY EARFSNLYVG TNGIISTQDF PRETQYVDYD FPTDFPAIAP FLADIDTSHG RGRVLYREDT SPAVLGLAAR YVRAGFPRSA RFTPTHAFLA TWEQVGAYEE VKRGALPSGE LNTFQAVLAS DGSDSYALFL YPANGLQFLG TRPKESYNVQ LQLPARVGFC RGEADDLKSE GPYFSLTSTE QSVKNLYQLS NLGIPGVWAF HIGSTSPLDN VRPAAVGDLS AAHSSVPLGR SFSHATALES DYNEDNLDYY DVNEEEAEYL PGEPEEALNG HSSIDVSFQS KVDTKHLEES STLDPHTKEG TSLGEVGGPD LKGQVEPWDE RETRSPAPPE VDRDSLAPSW ETPPPYPENG SIQPYPDGGP VPSEMDVPPA HPEEEIVLRS YPASDHTTPL SRGTYEVGLE DNIGSNTEVF TYNAANKETC EHNHRQCSRH AFCTDYATGF CCHCQSKFYG NGKHCLPEGA PHRVNGKVSG HLHVGHTPVH FTDVDLHAYI VGNDGRAYTA ISHIPQPAAQ ALLPLTPIGG LFGWLFALEK PGSENGFSLA GAAFTHDMEV TFYPGEETVR ITQTAEGLDP ENYLSIKTNI QGQVPYVSAN FTAHISPYKE LYHYSDSTVT STSSRDYSLT FGAINQTWSY RIHQNITYQV CRHAPRHPSF PTTQQLNVDR VFALYNDEER VLRFAVTNQI GPVKEDSDPT PVNPCYDGSH MCDTTARCHP GTGVDYTCEC ASGYQGDGRN CVDENECATG FHRCGPNSVC INLPGSYRCE CRSGYEFADD RHTCILITPP ANPCEDGSHT CAPAGQARCV HHGGSTFSCA CLPGYAGDGH QCTDVDECSE NRCHPAATCY NTPGSFSCRC QPGYYGDGFQ CIPDSTSSLT PCEQQQRHAQ AQYAYPGARF HIPQCDEQGN FLPLQCHGST GFCWCVDPDG HEVPGTQTPP GSTPPHCGPS PEPTQRPPTI CERWRENLLE HYGGTPRDDQ YVPQCDDLGH FIPLQCHGKS DFCWCVDKDG REVQGTRSQP GTTPACIPTV APPMVRPTPR PDVTPPSVGT FLLYTQGQQI GYLPLNGTRL QKDAAKTLLS LHVKWISPVG GRAAWLSQWE PPHRPCCSEV DWCREVLEGF //