ID H2NVW5_PONAB Unreviewed; 3076 AA.
AC H2NVW5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Laminin subunit alpha 1 {ECO:0000313|Ensembl:ENSPPYP00000010120.2};
GN Name=LAMA1 {ECO:0000313|Ensembl:ENSPPYP00000010120.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000010120.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000010120.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000010120.2}
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 AlphaFoldDB; H2NVW5; -.
DR Ensembl; ENSPPYT00000010522.2; ENSPPYP00000010120.2; ENSPPYG00000009019.2.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000157124; -.
DR HOGENOM; CLU_002471_2_0_1; -.
DR InParanoid; H2NVW5; -.
DR OMA; TVRQHVH; -.
DR TreeFam; TF335359; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005606; C:laminin-1 complex; IEA:Ensembl.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
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 GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 14.
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; 12.
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 PANTHER; PTHR10574:SF443; -; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 17.
DR Pfam; PF00054; Laminin_G_1; 5.
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; 12.
DR SMART; SM00180; EGF_Lam; 17.
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; 14.
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:UP000001595};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..3076
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035265085"
FT DOMAIN 19..270
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 398..454
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 455..503
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 524..709
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 743..791
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 850..902
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 903..951
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 952..998
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 999..1044
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1045..1090
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1091..1150
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1161..1362
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1404..1452
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1453..1509
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1510..1556
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2118..2298
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2306..2482
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2487..2674
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2714..2886
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2891..3071
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1709..1782
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 398..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 430..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 474..483
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 761..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 874..883
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 886..900
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 903..915
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 905..922
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 924..933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 952..964
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 972..981
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1017..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1045..1057
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1047..1064
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1066..1075
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1091..1103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1121..1130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1423..1432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1480..1489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1510..1522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1512..1529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1531..1540
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2647..2674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3076 AA; 337486 MW; 1650D1F14734CB82 CRC64;
MRWGVLGLAL LLCSVARCQQ RGLFPAILNL ASNAHISTNA TCGEKGPEMF CKLVEHVPGR
PVRNPQCRIC DGNSANPRER HPISHAIDGT NNWWQSPSIQ NGREYHWVTI TLDLRQVFQV
AYVIIKAANA PRPGNWILER SLDGTTFSPW QYYAVSDSEC LSRYNITPRR GPPTYRADDE
VICTSYYSRL VPLEHGEIHT SLINGRPSAD DLSPKLLEFT SARYIRLRLQ RIRTLNADLM
TLSHREPKEL DPIVTRRYYY SIKDISVGGM CICYGHASSC PWDETTKKLQ CQCEHNTCGE
SCNRCCPGYH QQPWRPGTVS SGNTCEACNC HNKAKDCYYD ESVAKQKKSL NTAGQFRGGG
VCINCLQNTM GINCETCIDG YYRPHKVSPY EDEPCRPCNC DPVGSLSSVC IKDDLHSDLH
NGKWPGQCPC KEGYAGEKCD RCQLGYKDYP TCVSCGCNPA GSASDEPCTG PCVCKENVEG
KACDRCKPGF YNLKEKNPRG CSECFCFGVS DVCSSLSWPV GQVNDMSGWL VTDLISPRKI
LSQQDALGRR HQVSINNTAV MQRLALKYYW AAPKAYLGNK LTAFGGFLKY TVSYEIPVET
VDSNLMSHAD VIIKGNGLTL STQAEGLSLQ PYEEYTNVVR LVPENFRDFH SKMQIDRDQL
MTVLANVTHL LIRANYNSAK MALYRLESVS LDIASPNAID LVVAADVEHC ECPQGYTGTS
CELCLSGYYR VDGILFGGIC QACECHGHAA ECDVHGVCIA CAHTTTGDHC EQCLPGFYGE
PSRGTPGDCQ PCACPLTIAS NNFSPTCHLS DGDEVVCDRC APGYSGAWCE RCADGYYGNP
TVPGESCVPC DCSGNVDPSE AGHCDSVTGE CLKCLGNTDG AHCERCADGF YGDAVTAKNC
RACECHVKGS HSAVCHPETG LCDCKPNVTG QQCDQCLHGY YGLDSGHGCQ PCNCSVAGSV
SDDCTDEGQC HCVPGVAGKR CDRCARGFYT YQDGSCTPCD CPHTQNTCDP ETGECVCPPH
TQGVKCEECE DGHWGYDVEV GCQACNCSLV GSTHHQCDVV TSHCQCKSKF GGRACDQCSL
GYRDFPDCVP CDCDLRGTSG DACNLEQGLC GCAEETGACP CKENVFGPQC NECREGTFAL
RADNPLGCSP CFCSGLSHLC SELEGYVRTP VTLGSDQPLL RVVSQSNLRG TTEGVYYQAP
DFLLDAATIR QHIRAEPFYW RLPQQFQGDQ LMAYGGKLKY SVAFYSLDGI GTSNFEPQVL
IKGGRIRKQV IYMDAPAPEN GVRQEQEVAM RENFWKYFNS VSEKPVTRED FMSVLSDIEY
ILIKASYGQG LQQSRISDIS MEVGRKAEKL HPEEEVASLL ENCVCPPGTV GFSCQDCAPG
YHRGKLPAGS DRGLRPLIAP CVPCSCNNHS DTCDPDTGKC LNCGDNTAGD HCDVCASGYY
GKVTGSASDC APCACPHSPP ASFSPTCVLE GDHNFRCDAC LLGYEGKHCE RCSSGYYGNP
QTPGGSCQKC DCNPHGSVHG DCDRTSGQCV CRLGASGLRC DECEPRHILM ETDCVSCDDE
CVGVLLNDLD EIGDAILSLN LTGIIPVPYG ILSNLENTTK YLQESLLKEN MQKDLGKIKL
EGVAEEMDNL QKKLTRMLAS TQKVNRATER IFKESQDLAI AIERLQMSIT EIMEKTTLNQ
TLDEDFLLPN STLQNMQQNG TSLLEIMQIR DFTQLHQNAT LELKAAEDLL SQIQENYQKP
LEELEVLKEA ASHLLSKHNN ELKAAEALVR EAEAKMQESN HLLLMVNANL REFSDKKLHV
QEEQNLTSEL IAQGRGLIDA AAAQTDAVQD ALEHLEDHQD KLLLWSAKIR HHIDDLVMHM
SQRNALDLVY RAEDHAAEFQ RLADVLYSGL ENIRNVSLNA TSAAYVHYNI QSLIEESEEL
ARDAHRTVTE TSLLSESLVY NGKAAVQRSS KFLKEGNNLS RRLPGIALEL SELRNKTNRF
QENAVEITWQ TNESLLILRA IPEGIRDKGA KTKELATSAS QSAVSTLRDV AGLSQELLNT
SASLSRVNTT LQETHQLLQD STMATLLAGR KVKDVETQAN LLFDRLKPLK MLEENLSRNL
SEIKLLISQA RKQAASIKVA VSADRDCIRA YQPQISSTNY NTLTLNVKTQ EPDNLLFYLG
SSTASDFLAV EMRRGKVAFL WDLGSGSTRL EFPDFPIDDN RWHSIHVARF GNIGSLSVKE
MSSNQKSPTK TSKSPGTANV LDVNNSTLMF VGGLGGQIKK SPAVKVTHFK GCLGEAFLNG
KSIGLWNYIE REGKCRGCFG SSQNEDPSFH FDGSGYSVVE KSLPATVTQI IMLFNTFSPN
GLLLYLGSYG TKDFLSIELF HGRVKVMTDL GSGPLTLLTD RRYNNGTWYK IAFQRNRKQG
VLAVIDAYNT SNKETKQGET PGASSDLNRL DKDPIYVGGL PRSRVVRRGV TTKSFVGCLK
NLEISRSTFD LLRNSYGVRK GCLLEPIRSV SFLKGGYIEL PPKSLLPESE WLVTFATTNS
SGIILAALGG DVEKRGDREE AHVPFFSIML IGGNIEVHVN PGDGTGLRKA LLHAPTGTCS
DGQAHSISLV RNRRIITVQL DENNPVEMKL GPLVESRTIN VSDLYVGGIP EGEGTSLLTM
RRSFHGCIKN LIFNLELLDF NSAVGHEQVD LDTCWLSERP KLAPDAEDSK LLPEPRAFPE
QCVVDAALEY VPGAHQFGLT QNSHFILPFN QSAVRKKLSV ELSIRTFASS GLIYYMAHQN
QADYAVLQLH GGRLHFMFDL GKGRTKVSHP ALLSDGKWHT VKTDYVKRKG FITVDGQESP
MVTVVGDGTM LDVEGLFYLG GLPSQYQARK IGNITHSIPA CIGDVMVNSK QLDKDSPVSA
FTVNRCYAVA QEGTYFDGSG YAALVKEGYK VQSDVNITLE FRTSSQNGVL LGISTAKVDA
IGLELVDGKV LFHVNNGAGR ITAAYEPKTT TALCDGKWHT LQAKKSKHRI TLIVDGNAVG
AESPHTQSTS VDTNNPIYVG GYPAGVKQKC LRSQTSFRGC LRKLALIKSP QVQSFDFSRA
FELHGVFLHS CPGTES
//
