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Database: UniProt
Entry: A0A2K6E8L4_MACNE
LinkDB: A0A2K6E8L4_MACNE
Original site: A0A2K6E8L4_MACNE 
ID   A0A2K6E8L4_MACNE        Unreviewed;       979 AA.
AC   A0A2K6E8L4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Nidogen 2 {ECO:0000313|Ensembl:ENSMNEP00000044486.1};
GN   Name=NID2 {ECO:0000313|Ensembl:ENSMNEP00000044486.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000044486.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000044486.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6E8L4; -.
DR   Ensembl; ENSMNET00000068997.1; ENSMNEP00000044486.1; ENSMNEG00000044801.1.
DR   GeneTree; ENSGT00940000157901; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000044801; Expressed in lung and 8 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
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; cd00054; EGF_CA; 2.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 2.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 2.
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; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR46513:SF15; NIDOGEN-2 ISOFORM X1; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF00058; Ldl_recept_b; 2.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 2.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00682; G2F; 1.
DR   SMART; SM00135; LY; 4.
DR   SMART; SM00211; TY; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 2.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51120; LDLRB; 3.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
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:UP000233120};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..979
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014321115"
FT   DOMAIN          121..351
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          352..393
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          394..436
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          441..484
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          485..521
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          530..598
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DOMAIN          609..677
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REPEAT          747..790
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          791..833
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          834..878
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          585..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..608
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        567..574
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        647..654
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   979 AA;  107980 MW;  F5436F1782C410FD CRC64;
     MEGDRVAGRP VLSPLPVLLL LPLLLSRAAA LHPDELFPYG ESWGDQLLQE GDDESSAVVK
     LANPLHFYEA RFSNLYVGTN GIISTQDFPR ETQYVDYDFP TDFPAIAPFL ADIDTSHGRG
     APHRVNGKVS GHLRVGHTPV HFTDVDLHAY VVGNDGRAYT AISHIPQPAA QALLPLTPIG
     GLFGWLFALE KPGSENGFSL AGAAFTHDME VTFYPGEERV HITQTAEGLD PENYLSIKTN
     IQGQVPYIPA NFTAHISPYK ELYHYSDSTV TSTSSRDYSL TFGAINQTWS YRIHQNITYQ
     VCRHAPRRPA FPTTQQLSVD RVFALYNDEE RVLRFAVTNQ IGPVEEDSDP TPVNPCYDGS
     HMCDTTARCH PGTGVDYTCE CASGYQGDGR NCVDENECAT GFHRCGPNSV CINLPGTYRC
     ECRSGYEFAD DRHTCILITP PPNPCEDGSH TCAPAGQARC VHHGGSAFSC ACLPGYAGDG
     HQCTDIDECS ENRCHPAATC YNTPGSFSCR CQPGYYGDGF QCIPDSTSSL TPCEEQQRHA
     QAQYAHPGAR FHIPQCDEQG NFLPLQCHGS TGFCWCVDPD GHEVPGTQTP PGSTPPRCGP
     PPEPTQRPPT ICERWRENLL EHYGGTPRDD QYVPQCDDLG HFTPLQCHGK SDFCWCVDKD
     GREVQGTRSQ PGTTPACIPT VAPPMVRPTP RPDVTPPSVG TFLLYTQGQQ IGYLPLNGTR
     LQKDAAKTLL SLHGSIIVGI DYDCRERMVY WTDVAGRTIS RASLELGAEP ETIVNSGLIS
     PEGLAIDHIR RTMYWTDSVM DKIESALLDG SERKVLFHTD LVNPRAIAVD PIRGNLYWTD
     WNREAPKIET SSLDGENRRI LINTDIGLPN GLTFDPFSKL LCWADAGTKK LECTLPDGTG
     RRVIHNNLKY PFSIVSYADH FYHTDWRRDG VVSVNKHSGQ FTDEYLPEQR SHLYGITAVY
     PYCPTGKKYA LGCSCKLAG
//
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