ID A0A7L1LKL5_HIMHI Unreviewed; 3156 AA.
AC A0A7L1LKL5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Laminin subunit alpha-2 {ECO:0000256|ARBA:ARBA00072595};
DE AltName: Full=Laminin M chain {ECO:0000256|ARBA:ARBA00079076};
DE AltName: Full=Laminin-12 subunit alpha {ECO:0000256|ARBA:ARBA00081478};
DE AltName: Full=Laminin-2 subunit alpha {ECO:0000256|ARBA:ARBA00082217};
DE AltName: Full=Laminin-4 subunit alpha {ECO:0000256|ARBA:ARBA00083678};
DE AltName: Full=Merosin heavy chain {ECO:0000256|ARBA:ARBA00076878};
DE Flags: Fragment;
GN Name=Lama2 {ECO:0000313|EMBL:NXN75600.1};
GN ORFNames=HIMHIM_R12413 {ECO:0000313|EMBL:NXN75600.1};
OS Himantopus himantopus (Black-winged stilt) (Charadrius himantopus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes;
OC Recurvirostridae; Himantopus.
OX NCBI_TaxID=225398 {ECO:0000313|EMBL:NXN75600.1, ECO:0000313|Proteomes:UP000571567};
RN [1] {ECO:0000313|EMBL:NXN75600.1, ECO:0000313|Proteomes:UP000571567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-13 {ECO:0000313|EMBL:NXN75600.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXN75600.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components. {ECO:0000256|ARBA:ARBA00002418}.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Alpha-2 is a
CC subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221
CC or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2
CC and NID2. {ECO:0000256|ARBA:ARBA00064740}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {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:NXN75600.1}.
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DR EMBL; VXBK01011032; NXN75600.1; -; Genomic_DNA.
DR OrthoDB; 10011303at2759; -.
DR Proteomes; UP000571567; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:TreeGrafter.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:TreeGrafter.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:0009888; P:tissue development; IEA:TreeGrafter.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 5.
DR FunFam; 2.10.25.10:FF:000106; Heparan sulfate proteoglycan 2; 2.
DR FunFam; 2.10.25.10:FF:000074; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000082; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000242; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000512; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000189; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000250; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000315; Laminin subunit alpha 2; 1.
DR FunFam; 2.170.300.10:FF:000008; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.200:FF:000052; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.200:FF:000057; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.200:FF:000061; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.200:FF:000063; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.200:FF:000065; Laminin subunit alpha 2; 1.
DR FunFam; 2.60.120.260:FF:000017; Laminin subunit alpha 2; 1.
DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000094; Laminin subunit alpha-2; 1.
DR FunFam; 2.10.25.10:FF:000128; laminin subunit alpha-2 isoform X1; 2.
DR FunFam; 2.170.300.10:FF:000026; laminin subunit alpha-2 isoform X2; 1.
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.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR050440; Laminin/Netrin_ECM.
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; IPR056863; LMN_ATRN_NET-like_EGF.
DR PANTHER; PTHR10574:SF291; LAMININ SUBUNIT ALPHA-2; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; EGF_laminin; 14.
DR Pfam; PF24973; EGF_LMN_ATRN; 2.
DR Pfam; PF00052; Laminin_B; 2.
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; 9.
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; 13.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
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 Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
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:UP000571567};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..249
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 377..431
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 432..480
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 501..685
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 719..768
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 769..826
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 827..879
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 880..928
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 929..975
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 976..1021
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1022..1067
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1068..1127
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1142..1376
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1417..1465
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1524..1570
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2140..2336
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2346..2525
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2530..2728
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2797..2968
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2973..3153
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2725..2781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3076..3095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1679..1800
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1978..2012
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2052..2135
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2733..2746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3081..3094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 407..416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 451..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 738..747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 797..806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 851..860
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 863..877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 880..892
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 882..899
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 901..910
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 929..941
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 949..958
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 994..1003
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1022..1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1024..1041
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1043..1052
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1068..1080
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1098..1107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1436..1445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1524..1536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1526..1543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1545..1554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2701..2728
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXN75600.1"
FT NON_TER 3156
FT /evidence="ECO:0000313|EMBL:NXN75600.1"
SQ SEQUENCE 3156 AA; 347834 MW; 39D4C1C99266DCEC CRC64;
GLFPAVLNLA TNALITTNAT CGEKGREMYC KLVEHVPGQP ARNPQCRICD QRSRVPHQRH
PITNAIDGKN TWWQSPSIQN GIEYHYVTIT LDLQQIFQIA YVIVKAANSP RPGNWILERS
LDGVDYQPWQ YYAITDSECL TRYNIHPRPG TPSYIKDDEV ICTSYYSKIH PLENGEIHTS
LINGRPSADD PSRVLLEFTS ARFIRLRFQR IRTLNADLMM FAHKDPNEID PIVTRRYYYS
IKDISVGGMC ICSGHAKACP LDPATNKSIC QCEHNTCGET CDRCCPGFNQ KPWHAGTFLV
KHECEPCNCH GKTEECYYDQ DVADRNQSLN VHGEYIGGGV CVNCTGHTGG INCETCVDGY
FRPEGVLPDS PDPCQPCSCD PNGSLHDTCV KDEKHAEGDM LPGFCHCKTG YAGESCNRCA
LGYTGYPECL PCNCSLKGSA NVDPCVGPCI CKEHVEGENC DRCKPGFFNL QQNNPKGCEE
CFCSGKTNVC THSHLTYKNI EDMNGWYLTD LPGLIRVTPK QKRFDGHQQF SISNVAARKV
LPQTYYWSAP SSYLGNKVTA AGGHLKFTVS YDFTEEETVQ LMVQSDVIIE GGNLRISTPK
GRIHLQPSEE HTEEIVLKPE SFFVHGTDVP VSRREFMTIL ANVKRILVRA TYSYGMNAIY
RLRSVSIEAA DHTSTGRKVA SAVELCDCPP GYDGTSCESC WPQHRRVNGT IFGGVCAPCT
CFGHAELCDD ITGECLDCKH NTGGSYCDRC LPGFYGDPTK GTAEDCQLCA CPLNIPSNNF
SPTCHFDRSR GLICDECPAG YVGPRCERCA EGYFGQPLIP GGSCQPCQCN DNLDFSIPGS
CDSLSGACLI CKPGTTGQYC ERCADGYFGD ALHARNCQPC NCHINGSFSE ICDSRTGQCE
CKANVIGRRC DVCQPETFGL QSSRGCVPCN CNSFGSKSFD CDGDGQCYCQ PGVTGKKCDR
CAHGFYNFEE GGCTPCECSH FGNNCDPISG RCICPPNTVG EMCDKCATNY WGHDLVSGCK
PCDCSLIGAL SSQCDLNTGC CFCRPEFSGD KCTECRLGYW HYPQCVACQC FLAGTDPQSC
DAELGKCSCI DHTGQCSCKV NVEGVHCDRC KSGTFGLSAR NPLGCSSCYC FGLTTQCSEA
RGLIRTWVTL KPEQMILPLV DEKLQRSTLS GIAFQPPEIV ANIEQVMQEL RSEPVYWRLP
EQFEGRKLTT YGGKLKYAIY FEAREETGFT TYYPQVIIRG GPPTHTRVIV RHMAAPLIGQ
LTRHEIEMTE HEWEYYGDDQ RFRNTVPWEY YHDDPGVNRT VSQADFTWKP YGDDSRPSRS
VTREDFLNVL YDVHYILIKA THGNIMRQSR ISEISMEVAE GGTVSGMTPQ AYLIEKCDCP
LGYSGLSCES CSPGFYRLPS SPAGRTPAPS LGACVVCQCH GHSTMCDPET AVCENCQHNT
AGHHCERCAL GFYGIVQGSP DDCQPCACPL SIASNNFSPS CVAEGPSDYR CTACPPGYEG
QYCERCSSGY TGNPQTPGGS CQECECDRYG SLPVPCDPLT GQCTCKPGFT GWKCVGCEHR
HARDGMKCIS CDDECTGLLL SDLDRLNQMI LSVNLSGPLP APYKMLHGFE NMTQELKHLL
SPQQAPERLL QLAQENLDTL VTEMDELLTR ATKVTADGKQ TRQDAERTND RAKSLGQFIK
GILQAAEAAN EEAIKLNETL RTQDDTLEKS LPELQSEADR MVAELRSRDL NMQERIAQEE
LKNAEDLLDK VKKLFGEPSE KNEDLKNEVR DKLANYHTKV DDARDLLREA TSKIREADRL
SAVNQKNMTM VEKKKQAVED GRQDVEKSLQ EGNDVLNAAN KLANEINLAI EYVEGVADKM
QPMSDQLKDK IDDLSQEIHD RMLPERVLQA ENHAAQLNES SAILDGILAE AKNLSFNATL
AFNAYTNIKD YTDEAEKVAK EAKAFANEAM QATSGPQGSL KDGAKSSLQK SFKVLNEAKM
SENNVKEKRN DLDSMQNRLK DADEKNSILL RALNETLGKL SAIPNDTAIK VQAAKDKARQ
ANDTGNDVLA QIKDLNQNLL GLRNNYSKLA DDVAKTNAVV KDPIKNIADA DSSIKTLEKE
ADRLLDKIKP IKELQDNLGK NISQIKELIN QARKQANSIK VSVSSGGNCI RTYRPEIKKG
TYNTVIVNVK TVVADNLLFY LGSAKFTDFL AIEMRKGKVS FLWDVGSGVG RVEYPDLTID
DGFWYRIEAS RQSVCLNYSV KIRRTGKNGT ISVRALDGPK ASIVPATFSA VSPPGYTILD
VDANAMLFVG GLTGKIKKSD AVRVTTFTGC MGETFLDSKP IGLWNFRDIE GDCKGCAVSP
QVADGEGTVQ FDGDSYAMVS RPIRWNPNIS TVMFKFRTFS SNALLMYLAT DDLKDFMSVE
LSNGRIKVSY DLGSGTASVT SNQNHNDGKW KSFTLSRIQK QANISIVDID TNEEETIATT
STGSHFGLNL KGHEKIYFGG LPTLRNLRPE VILKKYTGCL KEIEISRTPY NILSSPDFVG
LTKGCTLENI YTVSFPKPGF VELQPVSFDM GTEINLSFST KNESGIILFG TSGTVVPPRK
KRGYTGKKAA PLRRKRRQTG QAYYAVFLNR GRLEVHISTG IRDPHRITVK PEAGEFHDGR
AHSIRIERAK GMFTVQVDED KGQTQRLPTD QPISVKKLFV GGTSSQFQTA PIRNIPPFEG
CIWNLVINAT PMDFAQPVSF ENADIGRCPS LEPEVRSPED EDKPIHETVL IEPEPDTNGE
KERPGTTPAS PPPLAPSLSS ALDSCAADTE PAILEGGKQF GLSRNSHIAV AFDDTKVKNR
LTIEFEVRTT ADSGLMFYMA RINHADFATV QLKNGLPYFS YDLGSGNTST MISNKINDGQ
WHKIKVIRTK QEGNLIVDDV SNRTVSPKKA DILDVVGMLY VGGLPINYTT RRIGPVTYSI
DGCIRSFKMT ESPVDLDNPT SSFNVGKCFV TAQKGTYFDG TGFAKTVGAY KVGTDLLVEF
EFRTTRLNGV LLGVSSQKMD GLGIELVGGK VMFHVDNGAG RFSAIYEPDA PGSLCDGQWH
KVLANKIKHR LELTVDDRQV DSNSPNRAST SADTNDPIFV GGYPDGVTQF GLTTNIHFKG
CIRFLKLTKG TAKPQEINFS KALELKGVQP LSCPAN
//
