ID A0A1D1VTH3_RAMVA Unreviewed; 3718 AA.
AC A0A1D1VTH3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Laminin subunit alpha {ECO:0008006|Google:ProtNLM};
GN Name=RvY_12864-1 {ECO:0000313|EMBL:GAV02274.1};
GN Synonyms=RvY_12864.1 {ECO:0000313|EMBL:GAV02274.1};
GN ORFNames=RvY_12864 {ECO:0000313|EMBL:GAV02274.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV02274.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV02274.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV02274.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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:GAV02274.1}.
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DR EMBL; BDGG01000008; GAV02274.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VTH3; -.
DR Proteomes; UP000186922; 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: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; 21.
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; 20.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
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; 21.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00180; EGF_Lam; 21.
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 PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 16.
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};
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:UP000186922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..3718
FT /note="Laminin subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008898824"
FT DOMAIN 21..277
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 407..451
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 452..497
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 498..543
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 544..586
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 590..635
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 636..685
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 735..787
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1374..1419
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1420..1464
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1465..1511
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1512..1563
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1590..1764
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1798..1847
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1906..1957
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1958..2004
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2005..2051
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2052..2099
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2663..2861
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2880..3049
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3056..3230
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3359..3532
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3538..3715
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 3291..3311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 427..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 452..464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 454..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 473..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 520..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 544..556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 546..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 565..574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 590..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 592..609
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 611..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 636..648
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 656..665
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 758..767
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1374..1386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1376..1393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1395..1404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1437..1446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1487..1496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1515..1532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1534..1543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1817..1826
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1930..1939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1977..1986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2025..2034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2052..2064
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2054..2071
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2073..2082
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3203..3230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3688..3715
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3718 AA; 406157 MW; AC9BD18A6147B727 CRC64;
MGTNLIVFAM VLCCCERAYS QAAGLQPGQF NLATGRRISA TATCGEGEPE LYCKLTGANL
ERGDQQQRVG HEKYFVINGQ ICDYCDANSA DQSHPAENAN DGTERWWQSP PLSRGAQFME
VNLTIDFNQE FHVAYLLLRM GNSPRPEVWT LLRSNDYGKT WQPWQHFAEP SDCESYFGIE
PDQPILKDDD VICTSKYSRI VPLEGGEIVV SLVNDRPGRG NFLSNSVLQN WTKATNVRFQ
FQRMKTLLGH TTGVVRQDPT VTRRYYYSVR DISVGGLCVC NGHASSCDVQ DPNEPSRQLC
RCVHNTCGPY CDHCCPGFVQ KKWKPAMENS SNACEPCNCH GHSTECEYSA DVDEKHLSLD
IHGNYEGGGV CRNCRDNTEG INCEKCRNGY FHPKGKMKTD RDTCQICRCD PRFSTGNCAE
ITGICECKQN FTGTNCDRCN IGYFDYPTCK PCECNYNGTI NQVCNAGFGN CPCKPNYTGP
KCDQCMDNFF DFPNCTACDC DARGTVPGTT CERGTGQCVC TNNFGGRRCN QCADGYSGPN
CTPCDCDPSG TEKDICDKSS GVCKCKPGHT GPRCDQTAPG YFGRLPVARC NCDPAGSVND
VCDPVSGRCP CKNNYSGRAC DMCAAGYYKF PECLACNCDS YGTIGTTCDV RGQCQCKKNF
VGKTCNACAE GFYNYPLCEG CNCHPAGLIA SFGGCGKVEG ELCQCKERVT GRICDKCKPG
YWGLDLYNPS GCDECACNQD GTVSALSICD GRTGACPCKS NVEARQCTKC KDGFYKMDGA
NLHGCVGCGC DVGGAVSPVC DKNNGQCVCR PRINGKTCSQ VVKLHYFPTL HHLKFEAEDG
RAVENGPVQY EFKDSDFPGY SWRGYAVMSN KQQQIEIPVH IRKPSLYRML VRYANLANTT
ARADVIVIPE SNHRAEADQK AVVDFLPTRD GKYASVGEGT LTNTFVLHPG QWHVLMKTAK
PVLIDYIVLL PQAYYEATVL QEAVHDPCLY GQAHTCRNFT YPNLADKYIH VDPAVNSFYK
KNGDTLKPII DDSTRRGLKG ALIDASQPQL TMEAEILPTE PHHLVLAYFT RELNGVSGLN
ITVNKRTSTT PLEYRAALYN CPYEHVCRSV VLENGGKPAV FAPSDRYLRL TITPLGVNGV
QPDLVVTDLI AVPASEWHND HVRPQSGCVI VDGACVTGEF PAVPDSNVVE AETDTQISHM
RPEIPGLPAK VQTAMLYLTN QTSYLRGTTQ RAGDHVILVH YYQPNGAGGE FEAAVQGVES
NPATLETHFC PSLSGCRAVL RHAEGPGIGF RLGRDYSITI KGKDGHEVYL DYVIAVPANQ
YERRFLHETP RDLATSFINQ CSKDYFEIDP DVKGFCRQGT FSLVSAFNNE AMQCECNLEG
STSFQCEELG GQCQCRTNVI GRKCNRCKSG YWGFPECRVC NCPFNSVCDP VSGACICPPR
VMGERCDMCM PRTYGFHPIT GCQECNCNPY GTNGSLECDQ DSGTCFCKQN VGGRTCDKCI
TGYYSFPHCQ ACHYCDVRGA TDAICDQQNG QCLCKENVAG PRCDMCKAGT FLLDAKNPLG
CTKCFCCGVT SQCQPSAYSR VLLPLGDPQI ELAKWTTLPA LPVAMKSTGA EATVDPAVTS
NREVYWVAPT ELLGNRVTSY GGKLTYSINV AADGATGSLS PDVILKGRNM TIHYLHDTQP
VVGANHEVEV ELTEGNFEHE SGTKVSRDQF MMVMVALDAL HIKAGYFPNP RTLSLNYVTL
EGALPPKESN EIISGLNLAG KVEECVCPPQ YTGSSCEDCA PHHYRSKTGP YLGICLACDC
NNHAERCDPH TGQCINCLHN TTGERCDKCV EGFYGDATRG SPYDCMICAC PIPIASNNFA
TSCVVDQDGM GIQCTCRGGY VGDRCQYCAP GYFGQPEVPG GFCQPCQCNN NIDPNDPASC
DPITGACLKC LNNTSGPECN TCREDYFGDP TRSACQVCDC EAYGTESCNT TDGTCKCWPN
VEGLRCDRCA PDHWEFESGR GCSACNCQLG SKTKQCNVDN GQCDCRPGVI GKNCDRCASS
YWNYSASGCT RCACATKYSI GESCDPITGH CSCLPGVTGA ECDRCKPRHV LVENVGCEAC
GYCVHTLLDD FDEMNEKLDI ADREFEKVSA SQFATIRLNK LGQTIGNMSQ AVNFLTITGA
PQTLLGFDTQ LQAIESAVDK KHKQSGDARK TAEEKLKAAD QARDELSTLL RRAGGARRNV
TDLAQSFAVL EAYLRQGPGS KVQESTFLAE PILTTLRNRK FDDYRGNASF ELAAAKDTQS
SIRAFNTEHN GTLGRADALQ EGIRDFQEKM KDLEKWSVNA TETVAQARLK IEAVKENITD
NIEAIKVLKT IIADVQGNSS KKTAASQLFF TDAQTSFTTL DDQSRRLLTA RDQLNTTNRA
HFNDNRESLA SLSAAKNHTR MLEHEADRLD NMFKPTRNAA ALGKKAASVY GDIVDDVAAA
RAAYDNSTIL FNDITTASAN VRADVGDSLA KSQKLQDQAD QSKIDALKLR RTIDASRNKG
QVVNDRQAET GQVIAAFWTG MQQIPKDDLK AGLDDQTVRA NTADARATDI HAQAEKIIAE
LTGAPYGLNQ KPDDTVGLSE IMLLEKAAKQ APAEIPGFND RISRADAQIQ TNHAAADDLG
NKIAELRRKI DLTRSLTNRI KVGMELSRSN SVQLKNPSDI GRASTYTHIS LYFKTAERDG
LLYYLGNEVG TSRRVKRDFS PITDDYMALE IQNGFVVLLF DLGSGPTRVE VRDKFVSDNQ
WHQVIVERIG KTATVRVISL PGPDGRREFS AEGATSGPNT VFNLNQENST FFIGGMPLSF
RLQTPVKNKR FAGFIEGLEF DMEPIGLWNQ GNYTFDSSAP TVPQLAPERD QLLVPNVEEG
IKLDGNGYAV YNLEGRVDVA RDTAVILEMK TFDKQALLFM LGDDRSEEFF SVELNDGHVL
FQYNLGSGTT AIKSPGRYDD GKWHAIGVVR NGKRGVLQID SENVANDTSP GHEDRLDVNR
LMFLGGHPST RNTEITKQAF EGCVRSLEVD TRKVKLENTK EAKGALLGCP TTVKRMVTFS
DSSAGYLAMP AVNVESSFQI TLKFKTTTPN GLLFLTSSED NSQVLSLSLK DGRLVWASDD
GRGQVSSVTT DLDANWNGEW HYVSASKESN KMRLMIDDFE IVEASQAFVD SLHTVKPLYF
GGVPDDFQTT SPLRPQFRNF IGCIGDVVVN DRVQNFADSQ ERPGASYSAC AISAQPGQVL
PVLPPQPTAA TLAPFWQPPM MTTNLYQVVT MATARPGIFI SAGQINGATP ATTTTTTTTT
TTTTATTTQA TTAATRATTK LMGTTAILPQ PIPINTGSAT LTSCALPLQP DTDASDSTAL
QFGSRPESRQ EFSNAPATFM ERSDFSVEFK TTAEDGVLMY VDDQKPSPID FLAIYMKNGH
LVYAFNPGSG PAVVRSPLKY NDGEWHTVSA VKRNRLGQLI VDGTEVHSSE SPGTTEILNT
KFPLYLGGTN GNKNFSKNLE GVHLPFNGCL RNLRLNGVPF GNPSSTVAVG PCSERTEPGA
FFFQEGGHIS LRDKFVVGQD LDISIEIRPR SKDGVILAVG TSRRRRDYLA LQLVNGVVDF
SFDNGGGVTR VNVSLGSPFS MCDGDWHTIH AVKSKYVASL FVDDRFEDVK IGPAGQSAAD
TDLPLFLGSL PPSEPDMKIV ARKQYVGCMR NLKLNEQLEN FANGRVAGSV LSNSCPIA
//
