ID V8PHV8_OPHHA Unreviewed; 2967 AA.
AC V8PHV8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Laminin subunit alpha-3 {ECO:0000313|EMBL:ETE74129.1};
DE Flags: Fragment;
GN Name=LAMA3 {ECO:0000313|EMBL:ETE74129.1};
GN ORFNames=L345_00018 {ECO:0000313|EMBL:ETE74129.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE74129.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE74129.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE74129.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE74129.1}.
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DR EMBL; AZIM01000002; ETE74129.1; -; Genomic_DNA.
DR Proteomes; UP000018936; 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:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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 CDD; cd00055; EGF_Lam; 12.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 11.
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:SF434; PROTEIN TAG-53-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF02210; Laminin_G_2; 2.
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; 6.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 7.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
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:UP000018936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 48..301
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 431..474
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 475..520
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 570..622
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1185..1230
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1275..1323
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1324..1374
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1395..1574
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1687..1738
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2401..2604
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2613..2772
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2779..2949
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1840..1878
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1915..2024
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2053..2080
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2256..2290
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 450..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 475..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 477..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 496..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 593..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1185..1197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1187..1204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1206..1215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1299..1308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1324..1336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1326..1343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1345..1354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1687..1699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1710..1719
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1722..1736
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE74129.1"
SQ SEQUENCE 2967 AA; 332706 MW; 473FD601FA61930A CRC64;
MARTRVTAVL LTSRTPPGAA LARIVLALWS CCHPAGSLSA SSLGAGERAL SLHPPYFSLA
ETTRIWATAT CGQDESGRPR LELFCKLVGG PAASPAGQTI QGQFCDYCNA ADPNKAHPID
YAIDGTERWW QSPSLSLGLK YDEVNVTLDL GQLFHVAYVL IKFANSPRPD LWVLERSIDF
GRTYTPWQYF AYSKADCWER FRKEANSPLR KDNDVICTTE YSRIVPLENG EIVISLVNGR
PGANNFSHSS ILREFTKATN IRLHFLRTNT LLGHLISKAQ RDPTVTRRYY YSLKDISIGG
QCVCHGHADV CAGKTDPDSY RYQCECQHNT CGETCDRCCP AYNQKSWQPA TASSTNVCEP
CNCHGHALDC YYDHEVERRK ESLNLHGQYQ GGGVCIDCQH NTAGINCEKC LKGYYRPYGV
PITAMHGCIP CRCSPEHSNG CEEGSGRCYC QLNYQGETCD RCADGYHSFP FCYPCQCSTY
GSYQDTCHPT SGQCDCRPGF IGQKCDTCIT TSSTFPHCQG VIDECDPAGT RDSYSSYCQC
LQNVEGPTCS ICKPLYWNLA SANPYGCIDC QCDVAGVLSG IRECQQLAGE CYCKPYVCGG
PCDTCEAGYH GLETKNYFGC QGCKCDVGGS VSHVCNDLTG DCQCRSHIIG KTCIEPEKNY
YLPDLHHMKF EIEDGTSPNG RGVRFGYNSQ EFPGFSWRGY VQMSSIQYCT MSAWFQNTLK
GRSQLLRESI LTLITLNEVR ITLSVKKPKP YLFHVILRYI NPGTAVVSGH ITAYQSRTLK
VLLPSDYYEA SILQFPVVQP CTYSGYVITD NCLQYEYLPV DKYRCVFGTE VTFFLHKGQY
RKTTFQQPTV KHPVNLQIKL KVPQVGRYVI LFEYVTVYDL MYVGNIKTES LGQVMEAKIN
IYSCKYSFLC RSVVIDDMAR IAVFDLLADI TLHLRSSALD FLLHKICIIP IEDFSLDYVE
PQVYCIATYI HGSSASCIPL QYEKPLEAVV LDAHRDSKVV EGSRYVVSWD SLSSPLSSLH
SANGVILSSS QNQITLNGRV PHIGRYVFII HFYQPENPTF PVQVLVDGGQ LWSGSYNASF
CPHTSGCRSL LMSENHIEFD ILKHDISVTM KIPNERTMVL EHILVVPAHS YSYTLLHKDS
VIRSTDFISQ CGRNSFHIVP GNSSEFCRNS ARSLVAAFND GALPCNCHRK GATSATCNPD
GGQCNCRAHV IGRQCIRCQT GYYGFPFCKP CSCGRRLCDD ITGKCICPPQ TVKPRCEACM
RLHFGYHPLT GCEKCNCSSK GVTSAMNPEC NKIDGQCRCR SGIAGRQCDH CAPGSYDFPN
CKPCKCNRGG TEQDICNPQT GVCLCKENVE GVQCDMCRSG SFYLDPANPK GCTTCFCFGA
TNICHSTNKH RVKFTDMRNW HLEAVGNAMN IPTTFNPISN SVVADVQELP PFLHNLYWVA
PSSYLGNKLS SYGGYLSYQL KSFGLPSEGM TLLEKRPDVQ LIGREMKITY IDPNNPLPDK
LYYGSVQLVE ENFRHTSSNN LVSREELMMV LSRLDGLQIR GLYFTETQRL TLGDVGLEEA
TNTGNGNIAY AVEACSCPPE YMGDSCQECS PGFYHESVGQ FTGRCVPCNC NGNSDRCLDG
SGICIVSIYN KCCCKYSYYN FERNCLCLQK HKYLCGTNCQ HNTAGEKCER CKEGYFRDAS
QGFCKECHCP YTNSFASGCL EVNGEFQCFC KEGYSGKHCE SCAPGYFGNP LKYRYCQKCN
CLENGQLTKC DRLTGECISQ EPKDIDPNED CNSCGSCVIT LLEDLSTMGS ELRVIEFQMQ
SINTSAQLLG QMKHLEVRSK QLESLLDHSR SVVKTQSSKV DELETGLSHL NQNINALKEK
AEGNYKKAQT LLNNFSKTNQ RGRALISKIQ SILIHINVLL GQIDGTSTEG NSLPVNHSAK
ELVQAQQMIN EMRNRNFGQQ LTEAEKEKGK AQHLLDRIRN ELEKRKANNQ GLIKSVRDSL
NEYESKLNDL HESLREAKEQ TKLAENLNGE NKLLLEDIKK QTEEMTRQQS AMWDLLNSAK
ASVSQTNSIF ELFQKSKEEY ESLAANLDGA KKDLDEKLKS QFLSSSKEPL VVKAEMYANS
LQDLARKLKK NASKNELVTC TVGGATTFEN ISDIIKAAEA AANKALSAAD SASSKRIVTA
SLNLKGKSGL ILTNSKCSEF TQNSYSNSGT AGLDYEIALL LLCPYLAVLH FQIVDEKDLP
GMAERLKTNS GKVLNKARET QKTLQVDYFI DLSPGLDDMR NKLQEAERKK NAIQGNLSEF
QNNLQGIKRD NTESLITIAN TMIKNANNIT TNVLSELDPI KAGVENIKNT YENIQITDFN
KALTEASRSV NNLTNMLPDL FNKITNINQQ VISTSNITEN INRIRELIQK ARDAANKVAI
PMKFNGKSGV EVRLPDILDD LKGYTSLSFF LQRPDKKEHM TQPQTRNMFV MYLGNKDSSS
NYIGMAIRGG HLICAYNLGG SENEIRVTEK LYEKNTRDIA LDQVTFKRIY QYAELEYKHA
APSDLSAKYE PQDSSRNSNT LLNLDPDKVV FYVGGYPPEF TPPSVLDYPH YEGCVELDSL
NDRVFSLYNF KRTFNLNTTV VQPCRRYREQ SDEFYFEGIG YAHIKVSSDS ANIRYEQTIQ
TTSDVGLVFF AENQDKFISL RIENGSPIFT YKVDSQPPRE ISNGSMNNVT ENPVILHISP
KQYIFGVDKL RLYAIVNTFH FNSYYLGGIP TSLRERRFNI STPPFRGCMK NIKTSFERSI
SFSESFGVSR KCPDDWKLMR TANFFKNGVL DLSDEDFPFP DNFQVGFGFH TLAVNGMLLS
YNIRLADFTI FLRNGYVIVS LADEEIQSSK KCEIGSMHYI TVIKDDDTLK LLFDDMPNSK
TVVTPGRKSM NRPIKLGGNN FEGCMSNIFI ERTTKANAVE RITRYTPSKD FKGWKLSFVK
KLFNFYEFCY TVQLYIKFAI TYFYHEK
//
