ID A0A2Y9MEX4_DELLE Unreviewed; 3008 AA.
AC A0A2Y9MEX4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Laminin subunit alpha-2 {ECO:0000313|RefSeq:XP_022417592.1};
GN Name=LAMA2 {ECO:0000313|RefSeq:XP_022417592.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022417592.1};
RN [1] {ECO:0000313|RefSeq:XP_022417592.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022417592.1};
RG RefSeq;
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 RefSeq; XP_022417592.1; XM_022561884.2.
DR STRING; 9749.A0A2Y9MEX4; -.
DR KEGG; dle:111168261; -.
DR InParanoid; A0A2Y9MEX4; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000248483; 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: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; 15.
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; IPR009030; Growth_fac_rcpt_cys_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; 8.
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 SUPFAM; SSF57184; Growth factor receptor domain; 1.
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|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:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..172
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 300..354
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 355..403
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 424..609
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 643..692
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 693..750
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 751..803
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 804..852
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 853..899
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 900..945
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 946..991
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 992..1051
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1066..1265
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1306..1354
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1413..1459
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2031..2214
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2226..2407
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2412..2596
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2649..2820
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2825..3005
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1568..1643
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1676..1717
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1920..2026
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 300..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 330..339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 374..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 662..671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 721..730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 775..784
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 787..801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 804..816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 806..823
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 825..834
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 853..865
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 873..882
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 918..927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 946..958
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 948..965
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 967..976
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 992..1004
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1022..1031
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1325..1334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1413..1425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1415..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1434..1443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2569..2596
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3008 AA; 331579 MW; 83D98DCA8E5D722A CRC64;
MRTLWNSELH VVAVTLPQVF QIAYVIVKAA NSPRPGNWIL ERSLDDVDYK PWQYHAVTDT
ECLTLYNIYP RTGPPSYAKD DEVICTSFYS KIHPLENGEI HISLINGRPS ADDLSPELLE
FTSARYIRLR FQRIRTLNAD LMMFAHKDPR EIDPIVTRRY YYSVKDISVG GMCICYGHAR
ACPLDPVTNK SRCECEHNTC GDSCDQCCPG FHQKPWRAGT FLTKTECEAC NCHGKAEECY
YDENVARRNL SLNIHGKYIG GGVCINCTGN TAGINCETCI DGFFRPKGIS PNYPRPCQPC
HCDPIGSLSE VCVKDEKRAQ RGLAPGSCHC KPGFRGVSCD RCARGYTGYP DCKPCNCSGA
GSTNEDPCFG PCNCKENVEG GDCSRCKFGF FNLQEDNHRG CDECFCSGVS DRCQSSYWTY
GNIQDMSGWY LTDISGHIRV TPQQDDLDPH QQISISVVKA RQALPQSYYW SAPALYLGNK
LTAVGGQLTF TVSYDLEEEE EDTEHILQLM IILEGNDLRI STAQDEVYLQ PSEEHINVLS
LKEDLFTIHG TNFPVSRKEF MTVLANLKRV LIQITYSLGM DAIFRLSSVG LESAVPYPTD
RSIAAAVEVC QCPSGYTGSS CESCWPRHRR VNGTIFGGIC EPCQCFGHAE SCDDITGECL
NCKDHTGGLY CNKCLPGFYG DPTKGTSDDC QPCACPLNIP SNNFSPTCHL DRNLGLICDE
CPVGYTGPHC ERCAEGYFGQ PSLPGGSCQP CQCNDNLDFS IPGSCDSLSG SCLICKPGTT
GRYCELCADG YFGDAVDAKN CQPCLCNANG SFSEVCHAQT GQCECKPNVQ GRQCDECKPE
TFGLQSARGC IPCNCNSFGS KSFDCEESGQ CWCQPGVTGK KCDRCAHGYF NFQEGGCTAC
DCSHLGNNCD PKTGRCICPP NTIGEKCSKC IPNTWGHSIT TGCKPCNCSS VGSLDFQCNI
NTGQCNCRPK FSGAKCTECN RGHWSYPHCN PCDCFLPGTD DSTCDLETKK CSCTDKTGQC
TCKVNVEGVR CDRCRLGKFG LEAKNPLGCS SCYCFGATTQ CSEAKGLIHT WVTLKPEQTI
LPLVDEALQH TTIRGIIFQH PEIVAHMDLV RQDLHLEPFY WKLPEQFEGK KLMAYGGKLK
YTIYFEAREE TGFSTYNPQV IIRGGTPSHV RIIIRHMAAP LIGQLTRHEI EMTEKKWKYY
GDDPRISRTV TREDFLDVLY DIHYILIKAT YGNIMRQSRI SEISMEVAEQ GRITAMTPPA
HLIERCDCPP GYSGLSCEAC MPGFYRLRSE PGGRTPGPAL GTCVPCQCHG HSSLCDPETS
ICQNCQHHTA GDFCERCVLG YYGTVKGLPD DCQQCACPLI SSSNNFSPSC VTEGLDDYRC
TACPREYEGQ YCERCAPGYT GSPSSPGGSC QECECDPHGS LPVPCDPVTG ICTCRPGATG
QKCDGCKHWH AREGMECVFC GDECTGLLLG DLARLEQMAT SINLTGPLPA PYKILYGLEN
MTQELKHLLS PQRAPERLIQ LAEGNLNTLV TEMNELLTRA TKVTADGEQT GQDAERTNTR
ASSLGEFIKD LAQHAEAVSE KAVKLNETLG IQDKAFERNL QELQNEVDKM MTELRRKNLD
TQKEVAEDEL VAAEALLKKV KKLFGESRGK NEEMEKDLRE KLADYKSKVD DAWDLLREAT
DKIKEANLLS AENQKNMTAL EKKKEAIESG KRQTEDTLKE GTDILDEANR LADEINSVID
YVEDIQTKLP PLSEDLKDKI EDLSQEIKDR KLAEKVSQAE SHAAQLNDSS AVLDRILDEA
KNISFNATAA FKAYSNIKDY IDKAEKIAKE AKVLAHEATE LATGPQGSLQ EGAKGSLQKS
FGFLNEAKKL ANDVKENDEH LNGLTTRLDN ANVRNRGLLR ALNDTLEKLS AIPNDTAAKL
QAVKDKARQA NDTAKDVLAQ IKDLHQNLDG LKKNYNQLAD SVAKTNAMVK DPSKNKIIAD
ADATVKNLEQ EADRLIDKLK PIKELEDNLK KNISEIKELI NQARKQANSI KVSVSSGGDC
IRTYKPEIKK GSYNNIIVNV KTAVADNLLF YLGSAKFIDF LAIEMRKGKV SFLWDVGSGV
GRVEYPDLTI DDSYWYRIEA SRTGRNGTIS VRALDGPKAS IMPSTYHSAS PPGYTILDVD
ANAMLFVGGL TGKLKKADAV RVVTFTGCMG EAYFDSKPIG LWNFREIEGD CKGCTVSPQV
EDSEGTIQFD GEGYALVSRP IRWYPNISTV MFKFRTFSSN ALLMYLATRD LKDFMSVELT
DGHIKVSYDL GSGMASVVSN QNHNDGKWKS FTLSRTQKQA NISIVDIDTN QEENIATSSP
GNNFGLDLKA DDKIYFGGLP TLRNLSMKAR PEVNLKKYSG CLRDIEISRT PYNILSSPDY
VGVTKGCSLE NVYTVSFPKP GFVELSPVPI DVGTEINLSF STKNESGIIL LGSGGTPAPP
RRKRRQTGQA YYAIFLNKGR LEVHLSTGAR TMRKIAVKPE PSLFHDGREH SVHVERTRGI
FTVQVDEDRR HVQNLTVEQA IEVKKLFVGG APPEFQPSPL RNIPPFEGCI WNLVINSVPM
DFAQPVSFKN ADIGRCAHQK PPEDEDGAVP AETVIQPEPV PTPAVPAPTP VLAHAPCAAE
SEPALLIGSK QFGLSRNSHI AIAFDDTKVK NRLTIEFEVR TQAESGLLFY MARINHADFA
TVQLRNGLPY FSYDLGSGDS NTMIPTKIND GHWHKIKIIR IKQEGIIYVD GASNRTISPK
KADILDVVGM LYIGGLPINY TTRRIGPVTY SIDGCIRNLQ MAEAPADLEQ PTSSYRVGTC
FANAQKGTYF DGTGFAKAVD GFKVGLDLLV EFEFRTTRTT GVLLGISSQK MDGMGIEMIA
EKLMFHVDNG AGRFTAVYDA GIPGHLCDGQ WHKVTANKVR HRIELTVDGN QVEAQSPNRA
STSADTNDPV FVGGFPEGLN QFGLTTNIRF RGCIRSLRLT KGTGKPLEVN FVKALELRGV
QPVSCPAN
//
