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Database: UniProt
Entry: A0A151NYP3_ALLMI
LinkDB: A0A151NYP3_ALLMI
Original site: A0A151NYP3_ALLMI 
ID   A0A151NYP3_ALLMI        Unreviewed;      3663 AA.
AC   A0A151NYP3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Laminin subunit alpha-5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Y1Q_0002648 {ECO:0000313|EMBL:KYO41992.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41992.1};
RN   [1] {ECO:0000313|EMBL:KYO41992.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41992.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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:KYO41992.1}.
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DR   EMBL; AKHW03001485; KYO41992.1; -; Genomic_DNA.
DR   eggNOG; KOG1836; Eukaryota.
DR   Proteomes; UP000050525; 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: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; 19.
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; 16.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
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   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   PANTHER; PTHR10574:SF365; NETRIN-A-RELATED; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 20.
DR   Pfam; PF00054; Laminin_G_1; 2.
DR   Pfam; PF02210; Laminin_G_2; 3.
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; 14.
DR   SMART; SM00180; EGF_Lam; 22.
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; 19.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 9.
DR   PROSITE; PS50027; EGF_LAM_2; 14.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 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:UP000050525};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          13..266
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          396..440
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          462..508
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          509..554
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          555..599
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          600..644
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          645..690
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          742..794
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1400..1445
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1490..1538
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1539..1589
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1610..1788
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   REPEAT          1802..1850
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          1802..1850
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   DOMAIN          1822..1871
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1928..1981
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1982..2028
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2029..2075
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2907..3083
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3090..3258
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3312..3477
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3484..3660
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          3257..3294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2162..2210
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2266..2417
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2519..2647
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        416..425
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        462..474
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        485..494
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        509..521
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        511..528
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        530..539
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        555..567
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        575..584
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        600..612
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        620..629
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        645..657
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        647..664
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        666..675
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        765..774
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1400..1412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1402..1419
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1421..1430
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1514..1523
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1539..1551
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1541..1558
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1560..1569
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1841..1850
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1953..1962
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1965..1979
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2001..2010
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2049..2058
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   3663 AA;  403381 MW;  47B1F34247E15872 CRC64;
     MKNRTRDSAI AFICGRKAPG SDDDDGLRTR IAATATCGED GGALEDLYCK LVGGPVAGGD
     PHHTIQGQYC DICSSANSNK AHPISNAIDG TERWWQSPPL SRGLEFNEVN VTLDLGQLFH
     VAYVLIKFAN SPRPDLWVLE HSTDFGLTYE PWQYFASSRR DCIEKFGPRT VERVTKDDDA
     ICTTEYSRIV PLENGEIVVS LVNGRPGAMN FTYSPLLRNF TKATNIRLRF LRTNTLLGHL
     MGKALRDPTV TRRYYYSIKD ISIGGRCVCH GHADVCDAKD PNDPYRLQCD CQHNTCGGSC
     DRCCPGFNQV PWKPATSDSA NECQPCNCNG HAYDCYYDPE VDHHKASKSH EDMYEGGGVC
     IDCQHHTTGI NCERCISGYY KSPDHPIDSP YICYRCNCDS EFTDGTCEDL TGRCYCKPNY
     TGERCDACAE GYIDFPHCYP VPAFSHNDTG EQVLPAGQII NCDCYAAGTE GNACRKDSRT
     GVCVCKPNFQ GAHCDQCAPG HYGPSCQPCQ CSGPGQYEGT CDSETGQCLC RSGFEGQSCN
     QCAPGYFSYP LCQLCGCSAV GTLPGGCDSV GRCFCKPEFD GPHCDRCSTG YHSYPHCHAC
     SCDPRGSVDN TCSPAGQCRC HLNFAGHTCS QCAPGFYGYP SCTPCQCSAE GSLHGTCDQE
     MGQCSCRPKV TGLRCDTCVP GAYGFPHCEV GSCNPAGLES TDPSLPLGSC ACRAYVEGPA
     CDRCKPLYWN LTPENPYGCT SCQCNTKGTI SGVAECQQGS GQCFCKPNIC GQLCSTCKDG
     YFKLNRASYF GCQGCQCDVG GSVGPSCEKT GACHCRPNTR GPTCTQPAKD HYFPDLHHLK
     LELEEGTTPD GRAVRFGYNP LEFENFSWRG YAQMSPIQNK VRVTVAVKEA ELSLFHVILR
     YINSGGATVY GKITAFQPRR RGTEQTKQIV FAPSTEPAFV TVPQNSFGEP FVLNPSVWSL
     IVEAEGILLD YLVLLPSSYY EAPILQLKVT EACTYRPSPE QASRNCLLYK YLSADGFPSA
     SGADAVCRID NNLPRPCPVE LITPSHPRMV LCSGSDVEVQ VRLPIPQPGK YVVLVEYANT
     DGQQTAGVAV TSPQQAPQQG TSTFYTCDYS FLCRGMVVDS ENRLATFELR REATVRFTAD
     RAHVFLHKVY LIPHRRFTME FVEPKVHCIS LHGTFSPNSS SCVPSRFPKL SQSIVLEGGQ
     PVLIPLDLPL THAFSVTPTG PTTGPPPRPP TAVDSSAELI LLQPPQTAVV FNTRIQTLGR
     YTFILHCYQP NHPTFPVEVL INGGRIWQGQ ANATFCPHGY GCRSLVVAEN HIVLDVTDND
     LSVIIRVPED RQLWLDYILV VPEDSYSSQY LQEEPLDKSY DFISTCGVNG FYINPATSPR
     FCKDSAISLS LFYNNGAQPC RCHEVGAVSR QCEPFGGQCT CKSNVIGREC SRCATGYWGF
     PNCRPCDCGL RLCNEVTGQC ICPPHTIKPE CVVCEPQTFG CHPLVGCEDC NCSRPGVQEL
     TEPGCDVDSG QCRCKPNVIG RRCNLCAPGY YHFPDCRSCN CHPAGTEASV CDPVTGQCHC
     KENVEGPRCD QCRLGTFLLD ADNPKGCTKC FCFGATDRCH SVEKYRVEFS DMNGWRLLSS
     DRQEVGTSLR AEEDLVHADL KYLLEVYQEL YWQAPSSYLG DRVSSYGGHL RYELHSDARR
     GDVFVPMESR PDVILKGNQM SIMFREDTYP PPGDVHRGQL QLVEGNFRHT ETHNPVSREE
     LMMVLASLEQ LQIRALFSQI SSSIFLRRVI LETVTDSAVG IRASNVELCL CPANYRGDSC
     QECAPGYYRD TKGLFLGKCV PCHCNGHSDQ CLPGSGICIN CQHNTEGNRC ERCKDGYVDS
     YSPEGLLQCV GCPCPLSVAS NNFAVGCIRK GSTMQCLCKT GYAGAMCERC APGYYGNPLV
     IGSFCQPCDC SGNTDPNMLF SDCDPLTGAC SGCMHHTAGP RCELCAPGYH GDAVEAKNCT
     LCSCSPCGTE SCDPRTGRCL CKAGVTGQHC DRCQEGYYGY DSCSGCRRCD CDVGSLGASC
     HTQTGQCSCQ PGVNGARCHQ CAPGYWGLGE NGCTKCQCKG GSCDPRTGEC TCPSGLTGKQ
     CDTCIQQYEI PVASGPDSVR CEVCDTCVLL LLEDLRKIEA SFPTIRNQLI NLNASSIAWA
     RLHGLKNTME TLANHLREHQ RSMSGVRQRA EELVEENRDL TQDLNALQHK MTMTHRKANS
     LDEHTKNTYQ RVQQLLLNIR SIQNSIQELG HQMDMFGTGN VSATSTEEFR QKMAEVERML
     KEMRERDFSS QRGLAENEEE EAQKLLHRVQ NELHSKGEAN RALVNNIRDR LTQYNSELMD
     LRDALNEAVN KTRQTEDLNS MNLNNLEESQ RKKKELQKQH GLVQDTLRMA EDSLAQVSDL
     LQMIERAKED YEKLAALLDG AKHPLTERVK KFSPASSKIP VVEAAEEHAR FLDELARNLS
     SIIRSTNQDG FIQRAIDASN AYASIIEAVK KAETAAADAA DAASEALMGV VSGDLAAIAK
     KLKRNSSALE EAVRQEQRKL SGPIKGTLQA AREKVTDLRA RKDRLVTRLR AVQDMLEVDQ
     DGTKEAIQNA KDAAAKANET AARVQDTLNS MKKNLDEWKD QYGDLRNEDL HQAVQDAKKS
     VSSLESTIPL LLGKLSNLEN RKNKNATVSE NIVRIRQLIT QARNAASKVK VPMKFNGQSG
     VQVRSPSDLP DLAAYTSLKF YIQNPEPSSA SAPARRQGGP DEGRFVLYLG SKEGTGDYMG
     VVLKDRKVQW VYQLGDEEPT FLTIDEEIGE QFAVVSINRI LQYGHMSVTM EKKTLHETKG
     DSVAKGEQGL FNFDLHSVVF YVGGYPSSFM PPATLHYPGY QGCIELDTLN EEVVSLYNFH
     HTFHLDTATE KPCARSKSTG DPWLTDGSYF DGTGYAEIKF ESQIGPTKRF EQEMRMVSYN
     GILFFLEHEG QFLCLAVQDG KLVLYYDFSD GLKVAESNNN LALLTVSSTT NKAVQIYLLK
     MDNKKRILVR LERLTIFIVE QENSLENAVS YYLGGVPLSV LPESLKAIFP KGGSIRGCMK
     GLKALGKYVD LKRMTTTGVS YGCTSDLLVA RSVKLHGHGY LTLSLKNVPP LQDFYTGFSF
     RTSQSDGLLY YHATAEGKCQ VSLKSGQLAL EVLRTALTTQ NTYADDSSHY VAVYSDASGV
     RLYVDDELQE ATQAAEGASR QGLQEEQLRF QLGGLPETGA LSNLTGCIGN VFVRRKSDPQ
     MVVDLQQNVE SFNVTMSCPR DQQPQQMQVS PKKDRRKPKG PSRPSRLALK GRRQSQEMTC
     LLPRHPRAAR GAFQFGGFSM SRLEFDDIPE SFQEKSYFSM EVRLNATSGL LFYVASEQPG
     SFMAVLVSNG RFVLLADLGG NKLRIQSKDK YHDRRWHTVF FSRDGRRAQL VIDGLKAQDA
     TMATAGQFLX XXXLTWPRGA QLSWDTSVTS FSGCLRNLKL DQHPLPSPSR TFGVTRCYEG
     ALESGVFFAA EGGHVTLANA VSLEQDISLK LEVRPRSAAG LIFHIGRTRS YLSLSMDDKK
     VLLKANSGAG EFSTWVAHPA LCDGQWHAIT VTKQRNMIHV AVDRVGNNTV GPSQTHWAEH
     KEPLHVGRMP ETTKLGAASP SPLTPLPHYI GCIRNLMIDQ HLIDLPGTAT VRGSVGLRGC
     PVL
//
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