ID A0A0R3RFI4_9BILA Unreviewed; 3327 AA.
AC A0A0R3RFI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Laminin subunit alpha-2 {ECO:0000313|WBParaSite:EEL_0000012301-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000012301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000012301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) 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:PRU00460}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1147741.A0A0R3RFI4; -.
DR WBParaSite; EEL_0000012301-mRNA-1; EEL_0000012301-mRNA-1; EEL_0000012301.
DR Proteomes; UP000050640; Unplaced.
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; 16.
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; 13.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
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; 17.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 12.
DR SMART; SM00180; EGF_Lam; 16.
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; 7.
DR PROSITE; PS50027; EGF_LAM_2; 11.
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 Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..3327
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007428748"
FT DOMAIN 43..290
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 418..472
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 473..522
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 543..732
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 766..816
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 935..981
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 982..1029
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1030..1079
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1080..1127
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1175..1220
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1221..1277
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1289..1489
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1532..1580
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1581..1639
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2228..2428
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2440..2619
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2631..2825
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2973..3141
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3145..3323
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2880..2903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1907..1934
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1965..2007
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2168..2230
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 418..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 448..457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 493..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 785..794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 935..947
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 937..954
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 956..965
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 982..994
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 984..1001
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1003..1012
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1052..1061
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1092
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1082..1099
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1101..1110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1175..1187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1177..1194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1196..1205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1248..1257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1551..1560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1608..1617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2592..2619
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3296..3323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3327 AA; 372759 MW; 27EFD954265034AA CRC64;
MGSLAFLPHF FLTVAAILTA NFGGTVRIEQ EYDNYQEFTV VEGQHGLFPT IFNLATNGLI
YADATCGQHH REIYCKLVEH VFNRQPQCDV CDANDVRKRH PIEFAIDGTR RWWQSPSLAN
GLDYERVNIT IDLRQEYQVA YVIVKSAIAP RPGTWVLEKS LDGVNYQPWQ YYAVSDAECM
RQFNVPATTG VPRFTRDDEV ICTSYYSKLD PLENGEIYTS LVNGRPSAEA ASETLQQFTR
ARYVRLRLMS LRTLNADLMI INRRDKSNRL DLSVTRRYFY AIKDISIGGQ CICHGHAESC
PPDPVTGQSR CECRHNTCGE SCSECCPLFN QLPWRQGTQS RPNVCQPCQC FNHATRCEYD
EEVERLGLSV TPEGIFEGGG RCIACEHNTD GINCERCKWT YFRPAGVTHY REDACQLCDC
DPIGSEHNNC VRDETSADGD QKPGDCICKP GFGGRRCDVC APGYRNHPKC EPCPCNRAGS
LNFDTCEEEH CICKTNVEGL YCDRCKKGTI NLDIKNPEGC QPCFCFGLSK ECHEKQWNRG
EIRSTTGWVL TDLLGEKAVT PKSENEILMY TNNEYRNNDL YYWKAPKEFN GNLLNSYGGI
LQYYVYFVPM DNGQKTSIPD VIIEGNGVKV EYYSQQNFFP RENISIQIPM KEGSGWHNSH
MRTVIDKHEM MRVLADVNTL MIRAVYNREQ IQSSIYGLTL DTATGPKNTI EDEEEMLKSL
EASNALMRGV EVCQCPEYYA GNSCERCISG YRRVNNQLFN GRCEKCNCEG HSFECDPFTG
DCISCQHNTT GRRCHQCLPG HYGNPSLGGE LGQCRPCACP TIENSHSTQC SLTQLIVGSA
AAYGEDAYVC TACEHGYDGN KCEICADGFF GNPLAENGTC EVCDCNDNID PMTIGNCDRE
TGKCLKCIYN TAGDHCEECK ENHWGNPKDK SCRPCGCHPK GSHSATCNRS TGICDCHDNY
VGIQCNRCKD GHGDIENMCP PCNCNMTGSF SSECDEVFGQ CACKTGVFGK QCDMCRASYF
NFTENGCQFC HCNSFGAVDD GRCDNVTGKC ECRENVEGKM CEKCVDGYFN ITSGHGCQEC
ACDPLGSEGI QCDTHTGQCV CKSGVTGLKC DKCAPNHFGL DSNGCKECRV CPAPGHICDS
VTGECICPPN TVGEMCENCS KNAWNYDPLN GCILCDCSSI GADGPNCNPK NGQCNCRMGF
VGLKCDRCMH GHFNFPKCEL CNCDLSGTDP TTCENDSCLC DEKGQCSCKK NVVGLKCDSC
DAYSFSLEES NTFGCTDCFC FNRTNFCVQS SLVWQQIYAS DRQVIFSEPW KYYTRKHNLN
VLREDPPIYN SYPTDITPLY WPLPSSFLGD RTSSYNGFIR FTIKNDDNYR GVSNVAPDPQ
HFRFFPQVIM VGNHRIILEH TPDEMDESGR YKIRLHESQW RSRLSPDVRV TRKQLMIALQ
NLQGIYIRAT YNYPSTGDAA SINEISIDVA VWDNTTDPST NSIAIGVEQC ECPQGYDGNS
CQDPAEGYCR KRQPDFLNSP DDLALVGGPQ PCACNGHSTT CEAETCRCTN CEHNTYGDYC
ELCKPGYQGN ALIGGAACTK CACPLPDNSF SDTCLAVGHG RGYVCDACKP GYTGLYCENC
LSGYYGNPNI ETGQCECRPG LSGRDCSLCK DRHAFINGIC TSCDQGCTRD LMKEMDDLEE
LMKQQNFINL RPVPWKRVAR INNATKNLRL ILESVHLGSA IDENTSKTDL GMDDSFLDEV
NGLVEQTKFL LERTNKSKNT LQKSIGKAEK LSDRAREQDG ILRVVIGQLR NYINYGFERQ
DSSKISIWIQ EANNYVNAMK ERGIYIEKRY NRGNTDFEKS QDLMKLITSR MLNHTSFVEL
RKQLDVFGQW LHDYRDTIWD RARQDTVSAD KIAIIVAKRV DRFNAVKANI TALLAKATNE
LSEAENEVSI AKTEKILAMF DDFRLINETL LPEVDEMTRK CRDEADKYGQ LLDEYREEYV
EKSERHAAEL ENEAQKLQNS FADTKNAAAD PLRASNAYKE IVEALRNASK AAEGAKKAAE
FAYIDADPKS EISMVNMALQ AKNRSMAIKR QADELSLRDL ENERVTATDR VIELKKTLQD
SLKRKLAISE QYQSFDDQHD RMAGLISVAG DAEKRAKSVH QKMQEISIEI DTMSDAVSKL
QGFAGEGIRN VTNDVRKANQ GAQEAMRKVS EVKKQTDSDS KRISVLGEQI KLLQEKIKEA
REKASRIRIS MKSDENGNCR RSFISPAHLA PTNLFTIKYR PLRNVPDSLL FLTKTKTKRT
QQSEYIAMEL RDRRIVVQWN IGSGTRMATN THTINYIAPG DRTAWYHIVL ERFGNSVTLT
VALHHTISGE GERTIGEPTT VSVGQPDEDD SIIFNTVHGE TLIQFGIDAK LSQDLGLATN
KFLGTIGEFT VDGETLPLWA FAESTKVCEG HFAAPESQST GYFFRDGFAQ IHLPSTERPS
GAQITVILSA YSPDGLLYFR GNQESGDFIS LELRDGHVLF RINLGGDSYA IVKSKKSSYT
DGRLHTVRVI RNYEKIHLQV DDESDRNSVT IPGENARLNI NGDDHFVGGI PPGFSTTPFS
NFDIQWNGFF GCIQSVRPSQ VAELDLDNPI RSQRKLRGCT FKNGERLEPT DRVVGFNRPG
YLLIQGLQIS NNSTYVVSSN SHLHSARKLL MLHCCSNQAN WETFRKRRKI RNAFGNGYLA
FYLYRGYLVV HLGTDSSQKS KVLTLRSEVT YNDGQLHSIF FTRFETLVRL RVDDREIASG
TLGEQNTIGT ASSQLFIGGF PNGIKPSANE MPMAESMIGC VSNIFVDYRL VPIIPEAHIA
LIGSCPVEQI FSLQKSERRA DVEALQADEQ NAFNRKASKL SLHLTEPTLI TKTERLYADG
STKTNPVNIR EANNESEESE SNDFESVLIT TIASKISDIP TTVILAELTE KKDDDDDDDD
DGSATEFTAL TDFGPKKCGA NVLAQNDGEG AARFGIAEAS HSKLNFEEDH LDVNQFKIEF
AFRTVLPNGM LWVWANYNNY TRYFFLNIID GLVQLQVRGS KEPKILVYKS NKLNDGKWHN
ISMLKQGKGM LLKVDRNPAQ HLKDTPNPKV IRKRMYVGGV ISRHRKRFHL TVPSFSGCIR
NFVVNGMQYD LFEKSRHVVP CIVPSNSAYV HESGYMTFGS LKSIRQHGNI QISVQFRPAV
KDGFIFGLMA NKDPENARIA VYLKNSMMTF DFVFNNERRD LKHIFKKDLC DGAWHNVTLS
ISHSNAISIT VDGHRKRLSS KTSPESVEFF RSLPIYVGGV TATSASKIGL LSLIGCYQDL
QLHGKPVAFK YAKKLHKVLP DGCPFLN
//
