ID A0A3Q3N9Y2_9TELE Unreviewed; 2852 AA.
AC A0A3Q3N9Y2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Laminin, alpha 1 {ECO:0000313|Ensembl:ENSMAMP00000029074.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000029074.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000029074.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 STRING; 205130.ENSMAMP00000029074; -.
DR Ensembl; ENSMAMT00000029823.2; ENSMAMP00000029074.2; ENSMAMG00000019000.2.
DR GeneTree; ENSGT00940000157124; -.
DR InParanoid; A0A3Q3N9Y2; -.
DR Proteomes; UP000261640; 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 GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 16.
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; 14.
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; 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:SF409; LAMININ SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 16.
DR Pfam; PF00054; Laminin_G_1; 3.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 16.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1..247
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 375..427
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 428..475
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 494..675
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 709..757
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 758..815
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 816..868
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 869..917
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 918..964
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 965..1010
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1011..1056
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1057..1115
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1139..1330
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1373..1421
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1479..1525
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1900..2073
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2081..2257
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2264..2445
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2498..2667
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2672..2849
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1805..1895
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 375..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 403..412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 446..455
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 727..736
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 786..795
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 840..849
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 852..866
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 869..881
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 871..888
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 890..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 918..930
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 938..947
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 983..992
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1011..1023
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1013..1030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1032..1041
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1057..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1086..1095
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1392..1401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1479..1491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1481..1498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1500..1509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2418..2445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 2852 AA; 310744 MW; 79B3BC83632FD556 CRC64;
EIELYLFLFN AVITSNATCG DPEPEVYCKL VEHVPGRRIK NPHCAKCDAN SVLSKERHPI
TNAIDGTNQW WQSPSIKNGR QFHWVTITLD LKQIFQVAYV IIKAANSPRP GNWILERSLD
GMTFDPWQFY AISDSECLTR YNITPRLGAP TYKSDTEVIC TSYYSRLNPL EHGEIHTSLI
NGRPGSEDLS SDLLNFTSAR YIRLRLQRIR TLNADLMTLS TRDPREVDPI VTRRYYYSIK
DISVGGMCIC YGHAQSCPLD HVTKKLQCVC EHNTCGENCN ECCPGYHQQP WQPGTISKGN
TCEKCNCHNK AVDCFYNQTV AELFLSLNSH GVRRGGGVCI NCQQNTAGIN CETCRDGYYR
PAKTSPNSDS PCVECDCDLR GSKSSVCTRD DTQPGVSAGQ CVCREGFAGR QCDRCAFGYR
EFPQCVRCEC NLSGSINTDP CSPCTCKANV MGAHCDLCKP GFYNLQKENP LGCTDCFCFG
VSDVCEASTW STVFQTEAWL LPPQSIHTPP VIHGNELPIP GNTSSGHIHQ QLLSWTAPTS
FLGNKLVSYG GLLNYSVVYD VPLDNEDHSV PALTDIIIEG SGRTLRLWPP LPLLLSPLAE
RLVAVVIVPW RFVDDQTGVH ISRDDLLSVL ADTTSLSIQV HLNTSADEPI RLSSVSLDVA
DSGSASGVQA VAVEICECPW GYSGTSCEMC LPGFYRVGGV LFGGNCMPCE CNDHTTDCDV
NGLCLGCTHN TTGPHCEHCL PGFYGDATEA TPDDCRLCPC PLTEPSNRFS PTCVLDTSGQ
VSCDQCQDGY TGTNCERCAT GYYGNPQVVG GACVRCQCNN NVDVTEVGYC DTITGECLRC
RANTAGKHCE VCQPGYYGDA VHAKDCQECG CDVSGALSNV CDVTTGQCLC RENVTGRTCD
HCQVGFFGLE SGWGCQSCGC SQSGSLSQSC DEDGRCQCAE GLAGLKCDHC SRGYYGFRGN
GCTACTCDHT GGNCDPESGL CICPPHTEGD TCDRCETGHW GHDPITGCKP CSCSTPGSSA
PQCDLINGQC QCKKGFSGRS CDQCGPGYYG YPECFPCGCD MAGTEATFCN TTSGVCDCRQ
SGECVCKAGV SGRHCEECVS GWFGLSAESP DGCSRCFCSG LSRECEEQGG LTRASIALAR
PPPLLLLVTQ SNLQGEVSGV YQQGGDMLLE TRQLNGSRLV GPLYWRLPPQ FEGNQLLSYG
GLLSYIITFY AEDGSGLSNQ EPQVLMRGGT LRKLVIYTDM VAPSNEAMTQ HDIRMTEHKW
KYFNSVSEKV VSHTDFMSVL SNVQYIIIKA SYGTRLQQSR ISNITMETAI EVELTEESDI
RGGMVRLIES CVCPPGYTGL SCQDCAVGYF RQPWSELSPQ SQKSMFVRPC VRCRCSNHSD
SCDTETGDCQ DCQHHTTGRS CERCAPGYYG NVRGSIGDCS LCACPLRNNS FSPTCVAEGA
FGDFHCTACQ TGHEGRYCER CSFGYYGNPT LPGGMCSQCR CSGWGSLHLL CDALTGQCKC
KAGVRGQSCD QCDKRHILQG GKCVSCDDDC TGVLLGDLDN LHNHFLSVNL SAVAIAPYHH
LVVLENQTSD LQVQTHNTKA EHLNQTVEEE LDSANQTLLL EEVVSMLKTI KTVNLTAARN
TANQELRFSL VHSLQVDFLS NEMANKKLRP LSTSLIVGME MLKSTQTQLS DAEQQNVQTH
TRLDTVHTLL QQYQVSPLNM LTTAHTVYIC TCPTHPLLQQ VEVLTVELDQ WRPLLRKQVD
TLVVGLKMTD ALETVYRAEN HAHLLQSYAD SLASSMPPSS SSYQSESCRT SLLAQLRASV
AHSGLQAALQ RLQTLEEQLQ NSSSVVENTN NTVRETNMLM TNTHSAANEV EHKLEEAEHR
TDRLMQRIKP LSMLGETLSR NLSDIRELID QARRQAASIK VAVQADRDCV RSYRTQIQSS
NFNTLSLVLK TSSPENLLFY LGSNTTVDYL AVEMHNGKVS LVWNVGSGST RVDFPGLDIT
NNRWTRINAT RFGAHVSLSV HQLDSESAPL PIAKAKSLGS SRVLDIDKNS VIHIGGLPAH
TQVTHGCVGE ATINEKNIGL WNYISREGEC GGCFSSPQME ATSFHFDGSG FSLVQKSLRA
TSTSIVLLFK TLSPGGLLLY LASNNTRDFL SLELVEGHVR LTFDLGSGPL ILTSSRKYNT
GMWYKITLQR NKRKGYLSIM AADQSSEKEV LETESPGIAS DLNRSDLDPI YIGGLPPSRP
IRRQVVSRSY VGCIKNVEIA RSNFDLLKDA YGVRKGCVLE AVRSVSVLGG GFVQITPSSL
GHEVELLFTF SSNNQSGVLL AAFSDVHSQR QHFLSIQLVS GALEAGLGEV GGGTRFVTVT
KPYGGSFGDG EKHSVIITIN KKSLSLQVDE NHLKSVALLP DGFSPLSPAS FFIGGLPSGQ
ESLLPMRLQY LSRLFRGCIQ YLVVARALVD LSGATRYEGA EFNSCLLEER TGGAVLHDDL
DIDTTPDPAH LSVAPPTRLA ALTPGCASDD EPAFLPSAVQ FGLSRHSHMT FVINPNTVRK
SVSLKLSIRT WALDGLIFLL SDAKQMDFIV LKLMGGRLLM SADLGKGPAS ITSSVVINDG
EWHTVNAEVS RRSMSVSVGD LSPGSMTIKG NQLDVDNRLY LGGLPHTYTT RRVNVSSSFP
GCIRSVSLNR VKLDLSQSAS QHDVTSCFSK DQTGNYFNGS GYAVFMQDGY KVGSDVSIFL
EFRTSHLEGV FLGISSAKVD AIGLEMINGR VVFNVNNGAG RVSVLSTGQL LCDGRWHRLQ
ARKTKHILSL IVDGQTYTTL NPYPQSTSAE TNNPVYVGGY PDGVRQNCMS TSSRFTGCLR
NIQLVKSHLN DVLDPSSAHF LLGVTPNSCP VA
//
