GenomeNet

Database: UniProt
Entry: A0A1W4WA48_AGRPL
LinkDB: A0A1W4WA48_AGRPL
Original site: A0A1W4WA48_AGRPL 
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
//
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