ID A0A1W4WA48_AGRPL Unreviewed; 3720 AA.
AC A0A1W4WA48;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Laminin subunit alpha {ECO:0000313|RefSeq:XP_018320894.1};
GN Name=LOC108734014 {ECO:0000313|RefSeq:XP_018320894.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018320894.1};
RN [1] {ECO:0000313|RefSeq:XP_018320894.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018320894.1};
RG RefSeq;
RL Submitted (SEP-2023) 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}.
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DR RefSeq; XP_018320894.1; XM_018465392.1.
DR STRING; 224129.A0A1W4WA48; -.
DR EnsemblMetazoa; XM_018465392.1; XP_018320894.1; LOC108734014.
DR GeneID; 108734014; -.
DR KEGG; apln:108734014; -.
DR InParanoid; A0A1W4WA48; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR CDD; cd00055; EGF_Lam; 22.
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; 21.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
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:SF274; USHERIN; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 20.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 11.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 21.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 9.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 51..302
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 432..476
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 477..522
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 523..568
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 569..614
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 615..659
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 660..704
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1394..1439
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1440..1489
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1533..1583
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1604..1795
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1829..1878
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1937..1989
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1990..2036
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2037..2083
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2698..2896
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2901..3070
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3077..3246
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3366..3537
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3543..3717
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2535..2562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3327..3346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2452..2496
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2664..2691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 3330..3346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 452..461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 477..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 479..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 498..507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 523..535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 525..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 544..553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 569..581
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 571..588
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 590..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 615..627
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 635..644
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 660..672
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 680..689
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1394..1406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1396..1413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1415..1424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1457..1466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1533..1545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1535..1552
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1554..1563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1848..1857
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1961..1970
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1973..1987
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2009..2018
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2057..2066
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3219..3246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3690..3717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3720 AA; 411540 MW; 33CF6BDCDC7519B2 CRC64;
MGIVCKRLGF SFSSKIMFVV LRSRGRPLEA SPGLVSVLLT LSLTAGVANA RSDELTPPYF
NLAENRTIRA SATCGEDTEG PELYCKLIGA NAENDVNVNL IHGQFCDYCD PSRPDKRHPP
EYAVDGMETW WQSPPLSRGM KYNEVNLTID FGQEFHVAYI FIRMGISPRP GLWILEKSAD
YGKTWTPWQY FSDSESDCET YFGKETLRPI TSDDSVICTT EYSKIVPLEG GEIPISILNN
RPSARDYFNS PVLQEWTRAT NVRFRFLRTK NLLGHLMFVA RQDPTVTRRY FYSIKDISIG
GRCMCNGHAD VCEVTDPNDP NILLCRCQHN TCGPKCERCC PGFEQKAWQI SKNYAPFSCE
PCNCFQHSNE CVYDPEVDRK RLSLDIYGKY EGGGVCQNCQ HNTMGINCNQ CQPTFYRPYN
KHWNETDVCQ PCNCNYFYST GNCEEGTARC ECKPEYQAPN CDRCSYGYYG YPDCIPCGCF
LNGTESLQCE PVQGHCSCKY NFGGKYCKEC ADSYFNFPTC EPCGCNALGS ISDTCDQNTG
NCTCKSNYGG LKCDQCENGY FSYPSCTYCN CDIKGTEAEI CDKNTGKCLC KEGYGGERCD
QCIPGYFGYP ECKPCNCSVI GSASSVCDVS GTCPCLPNFG GRTCEQCRVG YYSYPECLAC
NCDGHGSIGV SCDNEGRCQC HNNFDGIRCE QCREGFYNFP ACEECNCNPA GVVAAFAGCG
SVPAGELCQC KERVEGRICD KCKPLYWNLN LNNPEGCSEC NCHIPGVLGG FAACDNLDGQ
CVCKPSVISR SCSECVAGTY DLQEENLFGC KDCGCDIGGS INTVCDKATG QCTCQARVTG
RTCKEPIQAH YFPTLYQFQY EVEDGHTPAN TAVRYGYDES VFPGYSWKGY AVFSQLQNQI
LYDVLISKPS LYLIILHYVN PNPETVTGTI RVIPDNPHSL EQTLQVHFKS SSEPAFVTAS
GATALVMEPG QWTVSIENKK NLFLDYFVLL PEEYSSASIL TQKVVEPCTI DDKTLCRDYS
YPNVSKFDVT LGNGGMVLRG DKVDPLKDFY GDHEHLIELK VLNRIPLLNK NQSEIAYNIT
IGKPGPYVLV INYFTPKGDH RTQTVNVESR AQNGVTRGRA LLYSCPYTMV CRQIVTDKKN
TLAIQNVDGN VINVILQGAD DANIGVQSIV AIPYDEWSLD YIKPRPVCIL KDGNCISSRY
PTPPESKKVQ FELDADVEGN VTRPVHKISN DSSYIYLEPS DNMIDLHAKV PVPGYYSFVV
QYYQPDNPEF NLNVIVQNGQ FYEAKLAVEH CPSKSGCRAV VKQADGNPFF SLTENFMITL
KAPNHKGVYL DYLLIVPADL YSENVLEEED LDRTAEFIST CASNHFYINT SDEGFCKDSV
FSITAGYNNG ALQCYCDHIG SLSFQCNKFG GQCECKPNVI GRQCEACKTG FYDFPDCKPC
NCPLTALCEA STGRCICPPH VTGERCDQCM PFTYGFDPII GCEECKCNPL GVEHNYLQCD
LFNGSCTCKN NVVGRTCSVC QAGYFAFPYC ERCDCNYAGT LPDICDQVSA ECLCKKNAVG
PDCSLCREGS YNLQADNEDG CTDCFCFGKT SRCTSSNYVQ SMIIDMQDWG LVEINETETS
SFDVTLLNST VYQGNAPTDI GVDLSQDDMK DKRVYFSAPS AYLGKKLTLY GSRLNYSIFY
TIGSSGKAVS GADVILAGAG THLAYMSVEQ PAVATDYSES LGIVESNFEL PSGIAAKREH
IMTVLNNLTG LYIRATYWSN TVTARLSNVL LVNGVPYNYT AMHGKIVQPA SSVEQCQCPP
GYQGLSCEDC APGYYRISTG PHGGYCVPCQ CNGHADECDV HTGLCFNCKH NTRGDHCEQC
DVGYHGNALQ GTPMDCLICA CPLPVASNNF ATACDLSSDG EKISCDCVEG YFGARCQSCA
PGYYGKPEVV GDFCKPCDCS GNIDPTDPYS CNTVTGECLH CLNNTFGNSC ALCAPDYYGD
AITAKNCQPC DCDNYGRERC DSHTGQCICK PNVEGEKCDR CVAEHYGFQS GQGCIPCNCS
PASLSAQCHD QTGQCQCKPG VTGRNCDRCT AGYWNFTSDG CISCGCKSEY SLGFGCNAET
GQCECLPGVT GEKCDHCPHR WAFVDGVGCH SCDSCTHDLL DDTDALAALI DPIIIEFNAV
DSGYFTTRRL THLNDTLNEL KPKVGKLQPN QINLSPVLGD LDKLETDVNS FNRKVLYAME
NSAVLADNAH NISLETDKVF DEISDAVVDA KYAVNYIESL SDSLISGEDK KVDAALEEAS
KLLDEINIFN LSGRANEADK QYLKADNLLE KLRNLKKPVD NIDDKAKMFK TNLTTINNKL
DDLANHTQFT FNTVLEVEKL LSKNRRNKDS VERKLDTIHT QTNDVEKNLK DSDVLLKNAS
EVLDNFKELI DGFPANPKEL EKSNLDFDNT LENNINQLVI VKDLVPVVKD HAQNLTLRAQ
ELDNLLTETR DLSENAVNAA NAYKNIVEEI KNARDAAVSG KSAAENAADI LNNISNQTID
ARNISTVLLE KAQKSHMETS QDLPPELEEA KSRSRPIRSL HEDNEEKLEN IRKILNNPIV
QPLELNIYQA AKTAEEADTI AQTTLDQATE TFKNIANEKT KSEHLPKDLD DTKRNILQVE
QQIYTVNQKL PNIVNSLKEF PDQYDSMRGT AQSVEDKIKK LNQQIALARD IANRIKVGVK
FYPNTTLELR NPPNLADLST STQISGYFKT SNPNGLLLYL GNGNGTKLRR TQTDDYLALE
IENGYPVLTL EIGNDPQRII SNKYVADDTW YQFIIDRTGH NAKLSIREEV AGGRDQIYTV
EETLNGTMTI FNLDRNLSKL FVGGYPPQFP MQNQVRQNSF DGEMEELVIG DTPISLWNFN
DGNENNHGAI ERNKLVNLQP STGYRFNGNG YAIINARLFN LRIRSHIKLS FKTFATEGLL
FLAGKEKTFI SIELRNGKIL YQYNLGDKTK TWYTKDTYND GKWHTVSASR DGANGNFIVD
EEEIPDRSPP VEGSAIEQVE TFSFGGYPQF HSFKDVTNTD FDGCIDNVTI MGNLVDLTQN
VKAYDVTPGC PVKFSRLVSF SENTNGYIRF GNISSGDIFQ LSLKFRTKEP NGLIFYFTNS
DQSVGLSLAL DEGELHLIDQ KIDIIPPDVT FNDNEWHVVT ITHNTTVLRL DYDDYAFQST
DSPPPLPRIL YGDFYIGGLP RTFAAKQGTV ATERNFAGCI GDTTVNGVIL NFANSTDKFR
EVIGKCILDK QIGSDTNIHV VPTLPPVEEL DFQTLAPSES FTRNPFIDAI PKRGDGGFES
GVHQPEEVVT TTSPATTTTT VATVIPDVRA PRPPGTPPPT IPQLPREPSC ALPIEPQYDD
TANSGSYRFG SDPESRLEYP EARGKYRKQF DFSLEFKTTE TGGILMYVSS IDHKQFAAII
LQSGHVVFIF SGGGAPAIIK SPGTYVDNAW HKVEVSRNHG DGKLVIDNEI AATGRAPSNT
AKIELSPPYY VGGIRSTDYE HALENLNTTR SLNGCIRDFH MNSKPMEKVK TFGAIPCSEN
VEPGTFFHQD EGYMKLKERF KVGVTINIKM DIKPRTTSGV LIAVHGKRDY LVLEMVNGTI
KVTVENGKGP ISNSFRADNP HYLCDGQWHT IQVIKSKSAV TLSVDATHTE PSVGDPHSIS
TDTGGGLFLG GHRLLHRARG ITVRKSFVGC MRSVFINEHP ITLSQDMAEG KVSVGFCPTN
//