ID T1FPL0_HELRO Unreviewed; 1472 AA.
AC T1FPL0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Laminin EGF-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=20210757 {ECO:0000313|EnsemblMetazoa:HelroP188055};
GN ORFNames=HELRODRAFT_188055 {ECO:0000313|EMBL:ESO12949.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP188055, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO12949.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP188055}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; AMQM01000273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB095811; ESO12949.1; -; Genomic_DNA.
DR RefSeq; XP_009009669.1; XM_009011421.1.
DR STRING; 6412.T1FPL0; -.
DR EnsemblMetazoa; HelroT188055; HelroP188055; HelroG188055.
DR GeneID; 20210757; -.
DR KEGG; hro:HELRODRAFT_188055; -.
DR CTD; 20210757; -.
DR eggNOG; KOG1836; Eukaryota.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; T1FPL0; -.
DR OMA; GECNMET; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 9.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00281; LamB; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 7.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101}.
FT DOMAIN 1..99
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 211..257
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 258..311
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 338..517
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 552..600
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 658..712
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 713..781
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 782..829
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 830..876
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 976..1021
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1146..1243
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 211..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 231..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 282..291
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 570..579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 682..691
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 754..763
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 782..794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 784..801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 803..812
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 830..842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 832..849
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 851..860
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1472 AA; 164675 MW; 48EAA5679D82ECEF CRC64;
MPAVRTAPLN NPSQVLCSED ESDISPLTDA SVVFTTLSKR MRPKKIPFDE LPALYEFTTA
SDIMISLIKM NTWGDEAFDE PRAQAQYFYA IKEINVGGRL ILMGIRWVSS GSVGILRCYC
QHNTDGVDCE KCLPFYNDLP WKRGTMREPF ECKPCNCNGL SDTCEFDADL YSQTGYGGRC
TDCRENTSGP HCEFCAVGFY KDHNYNRCFP CFCNIQGSVN EQCEMGGACL CKEGVHGEKC
DLCLPYHYNL TITGCDQCRC NYAGILEGTE RLCDANSGQC MCKEFVQGQN CDECKPGYFG
LAYDNALGCT KCFCYGHSSE CSLHDGYHIM EIKSSFRLGS DGWKGEAGSE DAVDVEHLSE
NNEITLGGAD AAARSHYFVA PANFLGDIHQ SHNLLLTFDL RISSSNRPVQ PQINDIMIVG
GNGVTLQTPI YSQGNPIPNE YVQHYKFVLG EHQNYQWHPI GMSNVEFARV LFNVTAIKIK
AVYSDDGAGF LSNVVLQTVS SSSYTENEGS NVVAVEFCKC PEGYVGQFCE SCAPGYKRHV
PHSGAFGVCV PCQCNGHSDH CEAESGQCMC EHSTTGTNCE LCMDGYYGNA MNGTADDCTP
CGCPDGNKCI FMEATQEVVC LDCADGYGGL QCDVCDDGYY AHGEYDGNSG TPLLCKKCQC
NNNADPNDVA QCHYETGKCL KCLYNTTGDA CQHCLPGFYG AAVDEPHGAC YACDCYHIGT
LPEELEVERN NQIENNGYIS NLLTCERDSG QCRCRDNVVG RRCDQCLDGT WNIASGEGCE
DCSCNLIGSF NSSCDVRTGQ CHCKPGVGGA KCDQCLPYYY GFSDSGCSKC SCDFYGSFSL
ECHNDTGLCP CRHNYEGRAC DQCAINRYNL KAGCVECPVC YGKVRDVYQG IQTDLNDIQR
LVLQAGNLTT VTLDDDDDPK LKDEVRQKVQ KLLESVKSSE ELDITLKLKN ECESIKELKA
KLDRVDYKIF HLNSTLKNAK KEVDTAESLL ESAEESIDEQ RKKLKKEGDE ELETIKRLKE
TSGRQSKEIT SLASDARSHV TLLKQQKEVM ENCSASFSNV TDEIHKIEIE LARQQINHTE
QMKNLNAVFE HSKNLLKIVQ KNSTDILAAS TIIHNDTHFF LKEVYDTEMP KINVDELSSA
VADIEAEEET SLVDKLSAEL SENKNEIERV RANVSDSTYQ MGLYLEEYND LKMQIELKFN
DANETEHSIK DTVTKSEETL NKLETFEAER QSKKKAADDA KTKLNDINLS VATSEKALTD
VSRDLWENNA LNDVTASASF LLDVMESFNK TKKIYENNVE TYMNSLNESE IMLAEHEVHF
AELDKAELLL NNFEEKNEEE YAKMEKIHID VGETLITLEE DIEYVCKEGE ENVNAVIHNL
NKLEPFNMAN FKRCQDEMEK NTDKLRMTNF NERFITLKER GDHYKKMTEA YREEMTRLTN
EVNMLETISK AIPWTCVTTE ELEVAPISWS NM
//
