ID A0A0R3S9V6_HYMDI Unreviewed; 3571 AA.
AC A0A0R3S9V6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Laminin subunit alpha-3 {ECO:0000313|WBParaSite:HDID_0000107101-mRNA-1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000107101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000107101-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; 6216.A0A0R3S9V6; -.
DR WBParaSite; HDID_0000107101-mRNA-1; HDID_0000107101-mRNA-1; HDID_0000107101.
DR Proteomes; UP000046397; 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 CDD; cd00055; EGF_Lam; 16.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 15.
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; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 15.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
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|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}.
FT DOMAIN 1..290
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 415..471
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 554..824
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 878..927
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 994..1040
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1041..1087
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1088..1139
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1140..1187
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1188..1235
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1282..1329
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1330..1387
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1709..1756
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1757..1811
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1812..1858
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 3169..3362
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 2225..2252
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 443..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 455..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 897..906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1012..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1024..1038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1041..1053
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1043..1060
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1062..1071
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1160..1169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1188..1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1190..1207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1209..1218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1305..1314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1358..1367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1728..1737
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1740..1754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1783..1792
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1795..1809
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1812..1824
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1814..1831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1833..1842
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3571 AA; 394534 MW; 49E544FCABD2539A CRC64;
LDMDPDSLLA EHAVITANAT CGERKREYFC RLVEHAGYNF AQVFQVNIAL LRMKRQAFSY
PQDARTFKDV DGTVIECNYC DARDPTLRHP IEYAVSGDNN LWWQSPSLAE GLQYHAVTID
VDLKQVYQIV FVLLRMGDSP RPANWILEKS IDGKDFQPWV FFAENAQQCI SMYQPTVNKT
LRITSDSRPH KLGNAEVYCT TYFSQPQNLQ AGEIIIPLTV DREGASASYF EASKPIDPEL
IEFLSARFVR LRFQKLQTLS GDWMTLRDQL DPTVYNRYYY SIRNIKIGGK CICNSHANTC
GRQIIDGVPR AVCDCQHNTC GYTCEKCCPL FNQQPWRPGG MCEECNCHGK ADSCVYNQTV
ANLLLSLNRY NVREGGGVCV GCREQTTGIN CEDCIPGYYR PLNVGPDAKN PCVPCQCNIY
GSTGVCISND ALMPEKQPGD CVCREGFAGR LCDRCAEGYY QSPIDPRGCL KCPCDVAGSH
RGQGYRCQPP CNCKANVDPD SLCKACLPKH FNLDDEDPEG CQECFCMGLT KDCQSVSVAT
ARRLEQEGKL GLVDTLEEWS LVVPSSPRSL SVPPTSAGAS ADEIETTRML RLSAEDAEFA
LGPPAAAPGR SIYWSAPAKY LGKQLTGYRG YLEVITRFTS PAIRTATAYD NYTASRVWIT
EPDVVIEVNT DCRIICTDAF SAMFKGHGIR LGYSPYPETR QTHRVQRIRL HESNFRVLVE
AGNGSLDRIP IHQTQATGNG RQQMYPDPTY GQDGSYRLDY TRVGRPATIV DIMTVLSNVT
KLYVKAKYTD DQTFTELRRV AMERAERKNT TLGGLPEGVR GIEECRCPPG HRGISCEECE
PGYWRDPSIA PAGDGQSGEI AAFLGLVNPI FRRACVPCDC NGRADTCDPN NGHCLNCKYN
TFGPKCEQCA PGFHIDPSKF GSDICQPCEC PSVLNQKTNS CVALSPGDLR TFGISAEKPY
ACLDCEDNTR GQFCESCIEM FYGNPLLGQP CRHCDCGPMA INCDSITGEC QCGHYTTGPR
CTECAPGSHG DPSRGEPCTP CGCHPVGSQS IECDKDTGLC LCRLFYEGRH CDRCVAGRGN
VEAGCPTCNC DPLGSVPQAN ASCDPVTGQC YCKPGVGGTL ECDRCADGYY NLGSNGCQLC
ECSNRALSTA CHPTTGQCEC GNNVIGQKCD RCLRGHYWNG SEPNCLPCEC GPGALVNNEC
DLYTGQCRCA LYVTGRRCDQ CQTGFWGPSP RGCQRCPQCP NGRVCDQLTG KCICPPNTIG
DQCETCSPNS YDYNPALGCK DCNCSSIGSV DPTGDCDLLT GQCACKSGFA GRACDECAPG
YYGYPNCKPC MCSLEGTLRN FSNGDQITCD PITGACLCKP NVEGEKCDKC IPGSFGLSAD
YPLGCYACFC FPTSQPAQCE QLKGFRSVPE AQRRLQLVGT DNQYMPGGPI VDLHLTSEVS
TGSSELPDLT VGQNQFKWRF SKSMPTYLIL PDVKGPHTRS YGSIFVEIHA DCLPTGNCGQ
EYPSTALQTR GRPSADRTVL EDPQKIFARM TALNGQLEFE YQPENLPTQT AIPGGDLAAQ
YNTIWMREAD WVLTRIRSQH LRVRPSRAAL VLGLTNITTF SVRLATPGIP LKAISVNYRI
RTAKSEALTQ LGTPITTIET CICNDTSTKG DHCELADELN YFPPITIKPG PDGTYFDDLF
DITKPSENGT IPAGGKPSFE IEGGSVLRCE CNGMASECDS ETGFCMNCEG NTAGAHCEVC
AEGYMGDPTQ GIPCERCRCP SENANFARTC HTIGQTGSYI CECLPGYAGQ LCDRCDTGYY
GDPVNMIPCK KCECNPAGSQ HQNCNMKTGQ CVCLPGVTGQ QCDECPPGHV VDGGRCIDCR
GECTGELLER AAEVSEKIDR IDLTELAHQG LGDLQNRTDK LLDRYESAGK ILNTERDLIE
RASKITSELT RISLNMMTSL PSSVKAIDEA SCLAANATNQ FSRDIVSLER KFNEWIQSMR
NLRPGQVDEI LIQHWHQTAR LIRQEIARLD LGLTSEWANK MLEDSRRLEE QLASIIKRTS
TADYGSKIDR LKYYQKLQDS HLTTQLEQLY LMGNQTQRGL DEIVSIHDMI DTTSGGALDT
LWVNQSRFEE ELNVLKSNAS DYQEPTMTEI SRLSDILENT QTFSEIPDTV PPDVISKAHS
LEMAKDRILA ALDRPGVDQT LEVREAYKKI ADTIWEARNI TDESMEAIEA SGGEGVSASS
IEASLADIMK RHDQATERVQ RLSDRLNDEQ LIIAANADRI TALKKSFVDI NAVLQRTLEA
SKLTADRVNK QLLPLVTLTR PQLDALAIET ANARKRFDAI DKEVKAIEKQ FNEMEGTANM
AVNQANSTQK SLLDAILATE ERVETVDRKM ADARRLASTA RSLLDLIYGS LGKDPIPLRL
NGGGDCVYTL IPYHATKSRV FDLEFWFAPA LQRISGTTGS ATGIRTNSVL LVGRRAFPAR
TSIFAVTVEP NGNLRFAWSQ PEVRVTAIPG RVDLYLQEIP KDRDNLEGLP IHQATYTDET
DSESLTTGLL LDNQLELRVG GAFHSVSAAG SNAPPMETWG DDGAEEIWNR LIKMEHAKGC
LYELKISGHR LGFPDFAKAD PACLQQTEDF CKIHTNFRPL VRDGYTWDKS ASLDKGLEIT
PSRKRPQQSA TDSSGSAQGV FLEYMQLLDF GAADSYARIT SYDHLSPCDR NLNIHLQKLA
PQKANSMVLT FYNYREDYGI TIESRGTELI WSRWQGNLKG GMGQRARGIR TNRVTPIAAN
YWALEEPMAQ DCALAKEDDY VFFVGGIPPG HFELRKAMKD YGLSTNGFRG RIGLATSGDN
LPGSLLIDSY TKTPIRNYGD TRFADIRQTE EDYVVANLAP ANQYCLTLMP LTNFTSFELK
PNKFSAPWLP EISMTVRFRP VGNDEINLLR MQVAEQNNLW FRVWLTSDLR VGIAIPSDPS
KFITREIFGA PVIRDPANNL AALKAREAQV FDQPLFTESV LSIQFAGHDN TILTVLFDQR
PVQTWTLSQP IAKSAVLQVY IGPELNTLSY SEFSISNLVI GRTRVDFAAE MVGSLRDKPF
YRFGECGSQL RPRFVALPAE SSPSLSSEFV YQGLDLPQPP SGRRVRSIFE DCGDINPQVC
EAISENVTKE WPSIIHSLLS PKPSRRVRVR SMQFSGNGQS SKNCRDTQNP SAWFNGEANW
EVQNIATLLN GKLDFRVTIG FRVRAIDDSK NTVGLLATFN FGFKAGILFI VLSERKVHLV
IESGADGNSD FYWSSPSLDL RSNAWHRLEL LPVSMQTSDS QNGVQITKMR FIFDYHDIII
EEPLTWRVPL NAFIGGYPTA RTLRIGSKTM NLGNLFGCVD ELTLGGQEFD LSKSGLPVCP
DCFALDTSAV HVLPKIQDII QPSRSLVLPL NLNINSKTLE GMNTVEFSFE VLYDTQKIGV
ESLFIMVFEN LDEPDSLVRL WVYLDRYMVY VSDGTMEEKV SFTVSSTEPI AWHYASIKVA
LQEIAAIIDI STQGESSQTA IIKAVGPLRA IYYGSDKEFT PEMQSEHHGG IVVPPFMGCL
RNLKLSVGEN TAVKVEFPEG TQHLVHGVCP L
//