ID V9K9W3_CALMI Unreviewed; 1255 AA.
AC V9K9W3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Nidogen-1 {ECO:0000313|EMBL:AFO94419.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94419.1};
RN [1] {ECO:0000313|EMBL:AFO94419.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFO94419.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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; JW861902; AFO94419.1; -; mRNA.
DR AlphaFoldDB; V9K9W3; -.
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; cd00054; EGF_CA; 3.
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; PF00008; EGF; 1.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 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; 3.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
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 2: Evidence at transcript 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1255
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004778000"
FT DOMAIN 107..274
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 404..444
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 448..681
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 682..723
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 724..766
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 771..814
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 815..851
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 858..927
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 998..1040
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1041..1083
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1084..1128
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 897..904
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1255 AA; 138728 MW; 602BF51A83805AEB CRC64;
MLVRRRRCTL QFELLLLLLL LLLQAVTVRS VSRSELFPHG EGVGDSLVEP GDDATSQPVR
LNQHLHFFDR AVSSLYVGTN GILTLDKPPR EVDYVDLFPP RFGAIAPFLA DLDTSDALGK
IFYRQDSTPY TLQRIALMVN QGFHQLSFIP ENAFIATWED VRAYKDLQQG DQPQSKRNTF
QAVLASDESS SYAIFLYPED GLQFYGTHAK AANNIDLELP ARVGFSRGES SFVLFTLEGP
SYAVTSSSEQ SVKNLYQDTN SGNRGVWVFQ LGSSTNSTIV PGEVSEHLAA ESIPNAFNIA
ATTIDHPSSR YLDVVENGPE NEDIELSEEF ATPLEPGVYK IDSQLDVKEQ PPKYPHYVEH
VPVPNPVEAQ QVQFEHPQFP NQRVELLDTE FDVTGNVFTY NTERQQTCAS SRDVCSNHAQ
CKDYPKGFCC HCSPGYYGNG KQCVAEGSPQ RVNGKVNGKI FVGNSPVPVE IEDIDLHSYV
VVNDGRSYTA ISRIPTALGW ALLPLSSVGS IIGWMFALEQ PGYENGFSIV GGEFTRRAEV
TFSPGNEKLV ITQQFSGIDE HHHLTIATTL EGRVPDIPAE STVHIEPYNE LYHHSSSAIM
TSSNVQYTIE PPGGATQERS FQLKQTISFH SCIHDDATRV MPATQQLTVD RTFVLYDRNE
QILRYAMSNK IGPVRDDSSD MNQNPCYTGT HRCDTNAACR PEEGNRFVCE CSAGFYGDGI
SCYDVDECRI DSTICGNHAE CNNQPGTFRC ECFSGYQFAA DGRTCVLIQR PVNPCQTGIH
SCDSPERARC IYTGDSGHIC TCLPGFTGDG KSCEDIDECQ PNRCHPYAQC YNTPGSFSCQ
CGPGYQGDGF QCTGSEGATQ CERHRDSVLE IPEPRGPRPT RYIPQCDGNG NYIPTQCHQS
TTICWCVDKN GEEIPGTRTH PGIRPPCLAT VVPPVVIGPT TRPDVIPLPP GTHLLFAQSG
KIEHVPVEAG GLKKGEAMTL LHVPDKIVIG VAHDCLEKMV YWTDIAGHTI NRASLQGGEP
VTVIRTGLES PEGIAVDHLG RNIFWTDSGL DRIEVAKMDG SQRRVLFSSG LVNPRAIVTD
SARGNIYWTD WNRDAPKIET SYMDGTNRRV LVKDDLGLPN GLTYDPFTSL LCWADAGTRR
LECMSPNQTG RRKVLEDIQY PFGITSYGRN LYYTDWRRDA VIAVDRISGR ESDEQQPRKR
SRLYGITVAY SQCPPGRNHC AVNNGGCTHL CLATPTGRSC RCPDTSVGVD CVERN
//
