ID A0A340XER3_LIPVE Unreviewed; 763 AA.
AC A0A340XER3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Protein kinase C-binding protein NELL1 isoform X2 {ECO:0000313|RefSeq:XP_007457694.1};
GN Name=NELL1 {ECO:0000313|RefSeq:XP_007457694.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007457694.1};
RN [1] {ECO:0000313|RefSeq:XP_007457694.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_007457694.1; XM_007457632.1.
DR AlphaFoldDB; A0A340XER3; -.
DR GeneID; 103069283; -.
DR CTD; 4745; -.
DR OrthoDB; 5487at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 6.20.200.20; -; 2.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24042; NEL HOMOLOG; 1.
DR PANTHER; PTHR24042:SF2; PROTEIN KINASE C-BINDING PROTEIN NELL1; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF00093; VWC; 2.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 4.
DR SMART; SM00215; VWC_out; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57603; FnI-like domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000313|RefSeq:XP_007457694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|RefSeq:XP_007457694.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..763
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016439257"
FT DOMAIN 57..227
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 271..332
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 434..475
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 476..516
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 517..547
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 549..584
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 645..703
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DISULFID 519..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 537..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 763 AA; 84469 MW; 1AACE26F672FB0BB CRC64;
MPKDVILIVW FCVCTARTVV GFGMDPHLQM DIITELDLVN TTLGVTQVSG LHNTSKAFLF
KDIEREIHAA PHVSDKLVQL FRNKSEFTFL ATVQQKPSSS GVILSIRELE RSYFELESSG
LRDEIRYHYI HNGKPRTEAL PYRMADGQWH KVALSVSASH LLLHVDCNRI YERVIDPPET
NLPPGSNLWL GQRNQKHGLF RGIIQDGKII FMPNGYITQC PNLNRTCPTC SDFLSLVQGI
MDLQELLAKM TAKLNYAETR LSQLENCHCE KTCQVSGLLY RDQDSWVDGD HCRNCTCKSG
AVECRRMSCP PLNCSPDCLP VHIAGQCCKV CRPKCIYGGK VLAEGQRILT KSCRECRGGV
LVKITEACPP LNCSEKDHIL PENQCCSVCR GHNFCAEGPK CGENSECKNW NTKATCECKN
GYISVQGDSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCVPGYIRVD DFSCTEHDEC
GSGQHNCDEN AICTNTVQGY SCICKPGYVG NGTICRAFCE EGCRYGGTCV APNKCVCPSG
FTGSHCEKDI DECALRTHTC WNDSACINLA GGFDCLCPSG PSCSGDCPHE GGLKHNGQVW
TLKEDRCTVC SCKDGKIFCR RTACDCQNPS VDLFCCPECD TRVTSQCLDQ NGHKLYRSGD
NWTHSCQQCR CLEGEVDCWP LTCPNLNCEY TTILEGECCP RCVSDPCLAD NIAYDIRKTC
LDSYGLSRLS GSVWTMTGSP CTTCKCKNGS VCCSVDLECL HNN
//
