ID A0A3Q3VVE3_MOLML Unreviewed; 3135 AA.
AC A0A3Q3VVE3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000000099.1};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000000099.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000000099.1}
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; 94237.ENSMMOP00000000099; -.
DR Ensembl; ENSMMOT00000000099.1; ENSMMOP00000000099.1; ENSMMOG00000000032.1.
DR OMA; SHSRINF; -.
DR Proteomes; UP000261620; 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:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 13.
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; 10.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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:SF291; LAMININ SUBUNIT ALPHA-2; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 14.
DR Pfam; PF00054; Laminin_G_1; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
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; 15.
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; 13.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 11.
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|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:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..282
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 471..519
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 539..722
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 756..805
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 806..863
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 864..916
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 917..963
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 964..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..1102
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1103..1162
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1173..1369
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1416..1464
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1523..1572
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2140..2323
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2333..2512
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2517..2714
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2775..2947
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2952..3130
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2738..2763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1822..1856
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1925..1998
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2052..2135
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 490..499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 775..784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 834..843
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 888..897
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 900..914
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 917..929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 919..936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 938..947
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 964..976
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 984..993
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1029..1038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1057..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1059..1076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1078..1087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1103..1115
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1133..1142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1435..1444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1523..1535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1525..1542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1544..1553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1556..1570
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2687..2714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3135 AA; 343643 MW; 9D3C197BF73A6C3E CRC64;
MLINSAVLSF LKALDVFFFL EVWLEEFLCQ QHDNKTHFLF SILIGSIYGD CVFFSGLFPA
VLNLASMSDI TVNATCGSLG PEMYCKLVEH VPGQPVRNPQ CRICNQRNTK PFENHPIEYA
IDGTNRWWQS PSIKNGMEYH YVTITLDLKQ VFQIAYVIIK AANSPRPGNW ILERSIDGVT
FHPWQYYAIT DTECLTRFNI NPRTGPPSYT RDDEVICTSF YSKIHPLENG EIHTSLINGR
PSRIRTLNAD LMTLTLRDPK DVDPIVTRRY YYSIKDISVG GMCICYGHAK ACPLNTVTKK
FSCECEHNTC GESCDHCCPG YHQQAWMAGT FHTRHICEKC NCHDKAEECY FNQTVADLSL
SLDIHGQRTG GGVCVGCRDN TAGINCQTCV PGFYRPSGVS ADEENPCIPC SCDARGSVSQ
SCVADSSQAT PSGFFMGAQG LYYTFSILTF FDSFVSRCAV GYMGFPVCLR CNCSVEGSTN
DDPCISPCVC KENVEGENCD RCKLGFYNLQ DDNWRGCEKC SCMGVASQCS ASTWTYQNST
LTGWHLVGHS GRTVWSVHRQ TPPYLSVRHS DVQSDLGSAY YWNAPGLYLG NKLSAYGGSV
VYTVSYNTDQ QEQVIIRVTS EPDLIIEGGG IKIIDKRFGQ PLYPSSPSTN RIALLPENFL
VADSVQPISR RDFLSVLANV TRVMVRASYS TERSAVYKLH SFSMQVANPA AEGHRRASAV
EICSCPPEYA GTSCEACISG FRRVNGILYN GVCEACHCHG HATQCDEVTG HCLDCSHHTM
GPHCDTCLPG YYGNATHMSP ADCQPCACPL NLLSNNFSPT CHLGKEGELL CDQCQLGYTG
PRCDRCSNGY YGQPTVPGSS CQPCDCHGNL DLSVPGSCDP ITGQCLRCRQ GYGGAACDSC
AEGYYGDAIT AKNCQPCQCH TNGSVSEVCN KKTGQCQCRE NVVGRQCEEC MTHGLTTGGV
CTPCHCNSFG SKSFDCDEIG QCRCQPGVTG PKCDRCARGF FNFQEGGCTP CQCSHLGNNC
DANTGQCICP PNTIGERCGR CAPNHWGHDI IDGCKDCGCS VIGSVTQQCN INTGCCSCRD
TFRGEKCNEC QIGYRDFPQC TQCECNFSGS DSQTCDLERQ VCACADRTGK CSCKPNVEGD
NCDRCKPDTF GLSLRNPLGC SKCYCYGLTQ YCTEAQGLIR MLLTLKPEQT VLTLVDKSNS
VETRRGVSFQ HPEILAHANL VTPALSEPYY WKLPEQFRGS MITAYGGQLK YAVYYEARDE
TGTSSYEPQV IIKGGPNRNI LMTRHIPGLQ IGQLTRHEID MTEHEWKYAD GRSMTREDFM
DILFYVDYIL IKASHGNLMR QSRISEISLT VAEEGRATKE SEEAHQIEKC DCPVGYSGLS
CEECAAGFYR LRAGSLASAP ASRVPTAAGM GSCVQCQCSG HSSTCDPETS ICQNCQDNTE
GDRCERCAPG FYGVVQGFHD DCKPCACPLT NPQNNFSPTC VAEGFDDYRC TACPEGYEGK
YCERCATGYH GNPQIPGGSC EECKCSLWGA LPGTCDPVTG QCRCRAGASG KSCDQCMDRH
VCGPTGIISC DDECSGLLIS DMDRLYRIIT DVTLTTPLPP PYKMLYRFEN MTEELKHMLS
PQKAPERLLQ LADSNLESLV VEMDQLHSRV TKVSADGEQV EDDADRIQKR AEDLEQFIRD
TLLGAKDLQL KGAEVNKTLS RKYGTPDKSL KDMKEDIQAM LAEMRKRQLG GKKSIAEEEM
EYGHAQTHTN THRSCMSLPH TAEIQILKKI NKKLSDHEGK LQEAQDLLYF AQGKTREAGS
LAEQNQANLT TLEVSKNRHA VFQEAQEVLA QGEKHLDEAN QLSDHINKEL EDLEGMGNEL
GLLHDRLDDK VNHLTNGLSD GGLANHVHDA EEHAKQLNES AAILDSILAE AKNLSFNATA
AFKAYSNIKA NVDEAEKEAK AAKQRASEAL TLALGPEVPV KEAAQGALQK SHRLLNQAKQ
LQNDVKENAD SVARLKGRVK AARDKTKNLL KAVNGTMETL NAIPNDTAAK LAATKAVAAD
ANTTAIDVLQ RLGDLNLQLH GLQRNYSELE ETVNTANQMI QDPEKNIHAA GAKVKDLEDE
ADRLLEKLQP IKKLQDNLRR NISQIKELIN QARKQANSIK VSVSSSGDCL RSYRPDIRKG
RYNTITLHVK TTTPDNLLLY LGSAKYVDFL ALEMRKGKVN FLWDVGSGVG RVEYPHHSIH
DGNWHRIEAS RNGLNGTIAV YPLEGSMAGM MPTLASANSP TAYTILDVDQ NAYLFVGGIL
GTVKKADAVR TSTFTGCMGE TFLDGKPIGL WNYRERQGDC KGCAVSPQRS DAEGTVQLDG
EGYAAVGRPT RWNPNVSTVA FNFRTFSSDA LLMYLATEDM KDFMSLELSE GKVKVNFDLG
SGVGGAISAN RHNDGSWKSL TISRNKKQAT VTVVDIDSGT EEKITATSQG SATGLNLRKS
QRIYFGGLPT IGNYRPEITL KRYAGCLREI EVSRTPYNLL SSSEYTGVTK GCNVENLYTV
SFSKPGYVEL AGVSLAVGTE ISLSFSTLAD TGTILLAVGG TSPVSKQVCF LFLFFFPFRR
RRQSGEPYLS VMLNKGTLEV LVYVGSNGLR RVVRRPDQGV LNDGREHSLR IERLPSSTFA
VQVDEEAKRE TTLPNDVPVN LQRIFLGGIP PEVEQTSNRA NVPFQGCIWN LMINTILSDF
SQPVSFENAE IGQCPNLAPP PPPPLLPEEE ELLRPTLKPT ETTPPAAPAA TPTAAAAPPT
AKQEPTVAPT VLEEAYQFGL SRNSHMTFAF DDAKVREKLI LEFGLRTKEE SGLLLYMARI
NHADFVSIQI KDGQVCLGYD LGHGNISACV PFSINDGNWH KIRVSRNKQR GLLAVDSKYS
KQMISPMKAD LLDVVGVLYV GGLPKNYTTK RIGPILYSIN GCIRSLKVMG GPLNMALPAS
SHMVGRCFVA TEAGTYFDGT GFLKAVPSYR VGLDVSIALE FRTSRTSGVL LAISNQASDG
LGLELVRGNL LFHVDNGAGR ITAEHVPEGG SFCDGRWHSV TANKLRHRVE LVVDGKQSQA
ESLNTRSNTC DTNDPLYVGG YPDGVRQAAL TTSTSFRGCL RNLKITKASK TMDVHFNKAV
EMKGVQPLSC PAVAA
//
