ID A0A182E2Y8_ONCOC Unreviewed; 3326 AA.
AC A0A182E2Y8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Laminin subunit alpha-2 {ECO:0000313|WBParaSite:nOo.2.0.1.t02341-RA};
GN ORFNames=NOO_LOCUS2341 {ECO:0000313|EMBL:VDK66090.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t02341-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t02341-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK66090.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:PRU00460}.
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DR EMBL; UYRW01000360; VDK66090.1; -; Genomic_DNA.
DR STRING; 42157.A0A182E2Y8; -.
DR WBParaSite; nOo.2.0.1.t02341-RA; nOo.2.0.1.t02341-RA; nOo.2.0.1.g02341.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
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:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 14.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR PANTHER; PTHR10574:SF448; WING BLISTER, ISOFORM B; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 16.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..3326
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041045843"
FT DOMAIN 42..289
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 417..471
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 472..521
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 542..726
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 760..810
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 929..975
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 976..1023
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1024..1073
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1074..1121
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1169..1214
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1215..1271
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1283..1482
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1525..1574
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2239..2437
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2449..2628
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2642..2829
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2972..3140
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3144..3322
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1760..1787
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1974..2016
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2086..2239
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 417..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 447..456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 492..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 779..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 929..941
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 931..948
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 950..959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 976..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 978..995
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 997..1006
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1046..1055
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1074..1086
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1076..1093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1095..1104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1169..1181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1171..1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1190..1199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1242..1251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1544..1553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2601..2628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3295..3322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3326 AA; 373333 MW; 8C631D30D4D39CCE CRC64;
MGFLAFLPKF LKISIILTAY VDGTKTAEQE YDSYQEFSVV EGQHGLFPTI FNLATNALIY
ADATCGQHHR EIYCKLVEHV FNRQPQCDVC DANDVKKRHP IEFAIDGTRR WWQSPSLANG
LDYERVNITI DLRQEYQVAY VIVKSAIAPR PGTWVLEKSL DGINYQPWQY YAVSDAECLR
QFGVPATTGV PRFTRDDEVI CTSYYSKLDP LENGEIYTSL VNGRPSAEAA SETLQQFTRA
RYVRLRLMSL RTLNADLMII NRRDKSNRLD LSVTRRYFYA IKDISIGGQC ICHGHAESCP
PDPVTGQSRC ECRHNTCGES CSKCCPLFNQ LPWRQGTQSH PNICQPCQCF NHATHCEYDE
EVERLGLSVT PEGIFEGGGR CVACKHNTDG INCERCKWTY FRPSGVTHYR EDACRPCDCD
PIGSEHNNCV RDETSADGDQ KPGDCICKPG FGGRRCEVCA PGYRNHPKCE PCPCNRAGSL
NFETCEEERC ICKANVEGIY CDQCKKGTIN LNMKNPEGCQ PCFCFGLSKE CHEKQWSRGE
IRNTTGWMLT DVSGEKMIAP KTESKVLMYT NSEHKNNELC YWKAPKEFNG NLLNSYGGNL
QYYVYFVPMG NGEQTFLADV IIEGNGIKLE YYSKQNFFPR ENISIQIPMK EGHGWQNAYM
RTPVNKHEMM RVLADVNTMM IRAIYNREQI QSSIYGLTLD TAIEPEDTPE RTESQASDSL
MRGVEVCKCP EYYAGNSCER CISGYRRINN QLFNGRCEKC NCEGHSFECD PFTGDCMNCQ
HNTTGRRCHQ CLPGHYGNPS LGGELGQCHP CACPTIENSH SAQCSLTQLV VGGVAAYGED
AYVCTACELG YDGNKCEICA DGFFGNPLEK NGTCKPCDCN DNIDPMTIGN CDRKTGKCLK
CIYNTAGDHC EECKENHWGN PKDKSCRPCR CHPKGAHSAT CNISTGICDC HDNYIGMQCS
RCKEGHGDIE NMCPACNCNR TGSFNSECDE VSGQCACKTG VFGKQCDMCR AGYFNFGDNG
CQFCHCDTFG AIDDGRCDNI TGKCECRKNV DGKMCEKCVD GYFNITSGQG CQVCDCDLLG
SEGIQCDAHT GQCVCKPGVT GLKCDKCAPN YFGLDLNGCK ECRVCPAPGH ICDSITGECI
CPPNTVGEMC ENCSKNAWNY DPLNGCTLCD CSGIGADGPN CNPENGQCHC QIGFVGLKCD
RCIHGHFNFP RCELCNCDLS GTDPTTCKNG ACRCDEKGQC KCKKNVVGLK CDSCDAYSFS
LEESNAFGCT ECFCFNRTNF CVQSSLVWQQ IYAPDRQVIF SEPWTYYTRK HNLNVLKEYP
LIYNSYPTDI TPLYWPLPPS FLGDRIASYN GFIRFTIKND DNYRGITNVA PDPQHFRFFP
QVILVGNHRI ILEHTPNEVN KSGRYRIRLH ESQWRSRLSP DVPVTRKQLM IALQNLQGIY
VRATYNYPTT GDTASINDIG IDVAVWENTT DTSNSVAIGV EQCECPQGYA GNSCQDPAEG
YCRKRQPDFL NSPDDLALVG GPQPCACNGH STTCEAETCR CTNCEHNTYG DYCQLCKPGY
HGDATIGSAN ACTKCACPLP DNSFSDTCFS VDHDRGYMCD ACKLGYTGLY CENCLTGYYG
NPNITGGMCQ ECACHQYGSK TGQCECRPGL TGRDCSVCKD RHAFINGVCT SCDQGCTRDL
MKEMDGLEEI MEKQNFTNLR PIPWKRAARI SNTTKNLHLF LDSLHFGDII GEDPSKTNIG
VDDKFLDDVH GLVEQTKFML DRTNKSKNTL QKNRAKTEEL SKRAREQDKI IRDVVSQLRH
YINYGSGKQD NSQINIWIQE ANGYLNAMKE RGIYIEKRYN RGNTDFEKSQ DLMKLITSRM
LNDTSFVELR KQLDVFEQWL NDYRDTIWDR ARQDTVSSDK VAIIVAKRVD RFNAVKANIT
ELLTKGTDEL SEAENKVTVA KTEKILTMFD DFKTINETLL PQIDETTKKC RDEADRYGQL
LDEYRQEYVE KNERHAEQLE NEARKLQNSF ADTKNAAANP LRASNAYKEI VETLRNASKA
AEGAKKAAEF AYIDADPNSE ISMVNMALQA KNRSVAIEGQ ADELSLKDLK NERLTTIEAI
NDLKETMQDA MKQKLTISEQ YQSFDDQHDR MTGLISVADD AEKRANDVHQ KMREISIEIN
TMSDAVSKLK GFAGEDIRNV TNEVRKANQE AQEAMKKVSE VKKQTDDDSK RISILGQQIK
LLQEKIKEAR EKASRIRISM KSDENGNCHR AFISPAHLAP TNSFTIKYRP LRNVPDSLLF
LTKTKTKRTQ QSEYIAMELR DRRIVVQWNI GSGVRMATNT HTINYIAPSD RTTWYHIVLE
RFGNSVTLTV ALHHTISGEG ERTVGEPTTV SVGKSDEDDS TIFNTVHGET LIQFGIDAKL
SQDLGLATNK FLGTIGEFTV DGETLPLWAF AESSKACEGD FAAPESQATG YFFRDGFAQI
HLPSTERPSG AQITVILSAY SPDGLLYFRG NQENGDFISL ELREGHVLFK INLGDDSYAA
VKSKKSSYAD GRSHTIRVIR NYDKIHLQVD NESDRNSVII PGQNAKLNIN GDDHFVGGVP
PGFNITAFRR FDIHWNGFFG CIQSVRPSQV AELDLDNPIR SQRKLRGCTF KNGERLEPTD
RVVGFTRPGL RLHSVRKLQM LRYCFNQAIW KRSENAEKLG NLLGNFEKLG ILLGLNVINQ
GYLAFYLYRG YLVVHLGTDS SRKSKVLTLR SEVAYNDGQL HSIFFTRYET LVRLRVDDRE
VASGTLGEQN TIGTASSQLF IGGFPDRVKP SANEMPIAEP MIGCVSNIFI DYRLVPIIPE
AHIALIGICP IEQIFSLQKS ERSADVETLQ GDEQNSFNRK ASKLSFHLTE PTLITKTERL
YADESIKIDR TNVGEVNNEP ESESNDLKTS AITATATIFN TIPIAQIPIE SVKKKDDDDD
DSATDFTTLT DLGPKKCGPN LLAENDGEGA ARFGIAEASH SRLTFEEDFL DVNKFKIEFA
FRTVLPNGML WVWAVYNNYT HYFFLNIMNG LLQLQVRGLN QPKILVYKSN KLNDGKWHDI
SMLKQGQEIL LKVDHNPAQY LKDVSNPKLL RKRMYIGGVI SRHRKQFNLT VPSFSGCIRN
FEVNDIQQDL FQKSRHVVPC TIASNSAYVH EGGYMTFGSL KSIRKIGAIQ ISIQFRPAVK
DGFIFGLMTN KDPENARIAV YLKNSLVTFE FVFNDERHDL KHVFKKNLCD GAWHNVTLSI
THSKMIVITV DGHRKRIPSK ISSESMEFFR SLPIYVGGAT ATSASKIGVL SLIGCYRDFQ
LHGKQIAFKD AKKLNKVLPD GCPFLN
//
