ID A0A287AKJ2_PIG Unreviewed; 1347 AA.
AC A0A287AKJ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Nidogen 2 {ECO:0000313|Ensembl:ENSSSCP00000044524.2};
GN Name=NID2 {ECO:0000313|Ensembl:ENSSSCP00000044524.2,
GN ECO:0000313|VGNC:VGNC:90743};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000044524.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000044524.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000044524.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000044524.2}
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 STRING; 9823.ENSSSCP00000044524; -.
DR Ensembl; ENSSSCT00000056085.3; ENSSSCP00000044524.2; ENSSSCG00000005030.5.
DR VGNC; VGNC:90743; NID2.
DR GeneTree; ENSGT00940000157901; -.
DR InParanoid; A0A287AKJ2; -.
DR Reactome; R-SSC-3000157; Laminin interactions.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000005030; Expressed in subcutaneous adipose tissue and 40 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd00054; EGF_CA; 1.
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; 3.
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; 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: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; 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; 2.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 4.
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 SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
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; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 1: Evidence at protein level;
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287AKJ2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1347
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036447019"
FT DOMAIN 106..272
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 545..775
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 776..817
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 822..865
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 866..902
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 911..979
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 989..1057
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 1127..1170
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1171..1213
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1214..1258
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 292..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 948..955
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1027..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1347 AA; 147948 MW; DDEA492F654D6927 CRC64;
MRGYRGARRP ALRAPPLLLL LLLSRAVALQ PDELFPYGQS LGDQLLQEGD DESSAAVKLA
LPLRFYDAQF SDLYVGTNGI ISTQDFPRET QYVDDDFPTD FPAIAPFLAD IDTSHGRGRV
LYREDTSPDV LSLAARYVRT GFPRSAAHFV PTHAFLATWE RVGAYEEPKR GAPPSGELNT
FQAVLASDES DTYALFLYPA NGLQFFGTRP KESYNVQLEL PARVGFSRGE VDDLKREEQY
FSLTSTEQSV KNLYQHSNLG IPGVWAFHIG SASPLDNVKP AIAGGDLSKA HPSVPLRHSS
SHAVAPEGED TEDNLDYYDE NEEEVEYPPG ETEEESNGHS PDDVSFHSRA DLKPSGGGIS
LPGSDLPSPL PRPTSRDGLE TESATLDPQT KEGRPQEEID APDLKGRGET SEQPGAQVPA
PPKTERDSPD PSWAALPPHP DEGALPAERD VPPVPSGGEV VLPNYPRRPD HAPPLGRGRQ
VVGVEDDIGS NTKVFTYNAA NRETCEHNHE RCSRHAFCTD YATGFCCHCQ SRFYGNGKHC
LPEGAPHRVN GKVSGHLLVG HTPVHFTDVD LHAYVVGNDG RAYTAISHIP QPAAQALLPL
MPIGGLFGWL FALEKPGWEN GFSLTGATFI HDMEVTFHPG GERVRITQTA EGLDPENYLS
IKTNIQGQVP YIPANFTVHI TPYKELYHYS GSAVTSTSSR AYSLTYGAIN QTRSYSIHQN
ITYQTCRHAP RHWAIPTTQQ LNVDRVFALY TDEEKVLRFA VTNQIGPVEG DSEPAPVNPC
YDGSHTCATT AQCHPATGVD YTCECASGYQ GDGRRCVVIA PPPNPCEDGS HNCAPTSQAR
CIHHGGRSFS CACLPGYAGD GHQCADVDEC SENRCHPSAT CSNTPGSFSC HCQPGYHGDG
FQCTPDPALG LKPCEHQQRE AQAQRTHPGA RLHIPQCDEQ GHFLPLQCHG STGFCWCVDP
NGQEVPGTRT PPGSLPPHCG PPEPTQRPRT VCERWRESLL EHYGGTPRDD QYVPQCDDLG
HFTPLQCHGK SDFCWCVDQD GREVQGTRSQ PGTTPACIPT VAPPTMRPTP RPDVTPPPVG
TFLLYAQGQQ IGHLPLNGTR LQKDMAKTLL SLHGSIVVGI DYDCRERMVY WTDVAGRTIS
RASLEPGAEP ETIVNSGLIS PEGLAIDHFR GTMYWTDSGL DKIERARLDG SERRALFHTD
LVNPRAIAVD PIRGNLYWTD WNREAPKIEM SSLDGENRRI LVNKDIGLPN GLTFDPFSKL
LCWADAGTKK LECTLPDGTG RRVIQNNLNY PFSIVSYADH FYHTDWRRDG VISVNRDSGQ
FTDEYLPEQR SHLYGITAVY PYCPTGK
//
