ID A0A1S2ZV30_ERIEU Unreviewed; 3077 AA.
AC A0A1S2ZV30;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Laminin subunit alpha-2 {ECO:0000313|RefSeq:XP_007525059.1};
GN Name=LAMA2 {ECO:0000313|RefSeq:XP_007525059.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007525059.1};
RN [1] {ECO:0000313|RefSeq:XP_007525059.1}
RP IDENTIFICATION.
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_007525059.1; XM_007524997.1.
DR STRING; 9365.ENSEEUP00000003128; -.
DR CTD; 3908; -.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; A0A1S2ZV30; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000079721; 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; 13.
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:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 15.
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; 7.
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; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling 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:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..250
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 378..432
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 433..481
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 502..681
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 715..764
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 765..822
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 823..875
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 876..924
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 925..971
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 972..1017
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1018..1063
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1064..1123
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1134..1337
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1378..1426
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1485..1531
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2103..2286
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2298..2479
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2484..2665
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2718..2889
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2894..3074
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1633..1845
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1946..2012
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2050..2098
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 378..390
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 408..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 452..461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 734..743
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 793..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 847..856
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 859..873
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 876..888
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 878..895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 897..906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 925..937
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 945..954
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 990..999
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1018..1030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1020..1037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1039..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1064..1076
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1397..1406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1485..1497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1487..1504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1506..1515
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2638..2665
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3077 AA; 339165 MW; 9C78435B4BD5A8B7 CRC64;
MGLFPAVLNL ASNALITTNA TCGEKGPEMF CKLVEHVPGQ PVRNPQCRIC NQNSSNPYQR
HPITNAIDGK NTWWQSPSIK NGIEYHYVTI TLDLQQVFQI AYVIVKAANS PRPGNWILER
SLDDVEYKPW QYHAVTDTEC LTLYNIYPRT GPPSYAKDDE VICTSFYSKI HPLENGEIHI
SLINGRPSAD EPSPELLEFT SARYIRLRFQ RIRTLNADLM MLAHKDPREI DPIVTRRYYY
SVKDISVGGM CICYGHARAC PLDPVTNKSH CECEHNTCGE SCDHCCPGFH QKPWRAGTFL
TKTECEACNC HGKAEECYYD ENIAIRNLSL NIHGKYIGGG VCVNCTQNTA GINCETCIDG
FFRPKGVSPN YPSPCQPCYC DPVGSLSEVC VKDVKHAPKG LAPGSCYCKS GFGGVICDRC
ARGYFGYPDC RPCNCSGIGS TNEDPCVGPC NCKDNVEGGD CNHCKPGFFN LQEDNPKGCD
ECFCSGVSNR CQSSYWTYDN IQDMNGWFLT DISGHIRVTP QKDFQEISIS TLEAQRSLPQ
NYFWSAPATY LGNKFTAAGG QLAFSFSYNS EEEDTQHTLQ IMVILEGNGL RISTVQDEVY
LQPSEEHINV FQLKEELFTK YGTNYPVNRK EFMTVLANLK RLLIQITYSL RMDAIFRLSS
VDLEYAVPYP TDGSIASAME VCQCPPGYAG SSCESCWPRY RRINGTIFGG ICEPCQCFGH
AESCDDITGE CLNCKDHTGG PYCSQCLPGF FGDPTKGTSD DCQPCACPLN MPSNNFSPTC
HLDRSLGLIC DECPDGYTGP RCERCAEGYF GQPSVPGGSC QPCQCNDNLD FSIPGSCDSL
SGSCLICKPG TTGRYCELCA DGYFGDAVDA KNCQPCPCNV NGSFSEVCHT RTGQCDCKPN
VQGWRCDECK PETFGLQSGR GCIPCNCNSF GSKSFDCEEN GQCWCQPGVT GKKCDRCAHG
YFNFQEGGCT ACDCAHLGNN CDPKTGQCIC PPNTIGEKCS KCAPNTWGHS IVTGCKACNC
SAVGSLDFKC NRNTGQCNCH PKFSGAKCTE CRRGHWNYPH CIPCDCFLPG TDSTTCDSET
KECYCSDQTG QCTCKVNVEG IHCDKCQSGK FGLDAKNPLG CSSCYCFGVS TQCSEAKGLI
RTVLTLQPQQ TILPLVDEAL QHTTTKGIAF QQPEIIAHMD PVRQDLHLEP FYWKLPEQFE
GKKLMAYGGK LKYAIYFEAR DEIGFSTYKP QVIIRGGTPS HARIITRHMA APLIGQLTRH
EIEMTEKEWK YYGDDPRVSR TVTREDFMDI LYDIHYILIK ATYGNGMRQS RISEISMEVA
EQGHRTAVTS PAHLIERCDC PPGYSGFSCE TCMPGFYRLR SESGGHTPGP TLGTCVPCQC
NGHSSLCDPE TSICQNCQHH TAGDFCERCS LGYYGIVRGS PNDCQQCACP LTSSSNNFSP
SCVMEGLDDY RCTACPRGYE GQYCERCSPG YTGSPSSPGG SCQECECDPQ GSLPVPCDPV
TGICTCRPGA TGQKCDGCRQ WHAREGMECI FCGDDCTGLL LGDLAVLEQM AMSINLTGPL
PAPYKMLYDI ENTTGELKHL LSPQRAPERL TQLAEGSLST LTTEMNELLT RATKVTADGK
QTGQDAERTN GRASSLRESM KKLVQDAEAV NEKAVKLNET LGTQDKAFER NLQELQKEID
QMLTELRRKN LDTQKEVAED ELVAAEGLLK KVKKLFGESR GKNEAMEKNL RERLEDYQNK
VDDAQDLLRE AVEKIREANR LSAINQKNMT ALDHKKEAIE SGKQQIENTL KEGSEVLDEA
SRLANEIKSV IDYVEDIQTK LPHMSDELKS KIDELSQEVK DRKLAQKVSQ AESHAAQLND
SSAVLDGILD EAKNISFNAT AAFKAYSNIK DYIDEAEKIA REAKGLAHEA TKLATHPDGS
LKEVAKSSLQ KSFGILNEAK KLANDVKEND DRLNGLTARL ENADAQNENL LKTLNDTLGK
LATIPNDTAA KLQAVKDKAR QANNTAKDVL AQIKDIHQNL HGLKRNYNQL ADSVAKTNAV
VKDPSKNKII TDADATVKNL EQEADRLLDK LKPIKELEDN LKKNISEIKE LINQARKQAN
SIKVSVSSGG DCIRTYKPEI KKGSYNNIIV NVKTHVADNL LFYLGSAKFV DFLAIEMRKG
KVSFLWDVGS GVGRIEYPDL TIDDSYWYRI EASRTGRNGT ISVRALEGPK ASIVPGTYHS
VSPPGYTILD VDANAMLFVG GLTGKLKKAD AVHVITFTGC MGETFFDSKP IGLWNFQEKE
GDCKGCTVSP QVDDSEGTIQ FDGEGYALVS RPIRWYPNIS TVMFKFRTFS SSALLMYLAT
RDLKDFMSVE LTDGHIKVSY DLGSGMASVV SNQNHNDGKW KSFTLSRIQK QANISIVDID
TNQEENIATS SSGNNFGLDL KADDKIYFGG LPTLRNLSMK ARPEVNLNKY SGCLKDIEIS
RTPYNILSSP DYVGVTKGCS LENVYTVSFP KPGFVELPPV SIDVGTDINL SFSTKNESGI
ILLGSGGTLR RKRRQTGQAY YAIFLNKGRL EVHLSTGTRT MRKIVVKPEP SLFHDGREHS
VHIERNRGFF TVQVDENRRH MQNLTIDQAI EVKKLFIGGA PPEFQPPPLR NVPPFDGCVW
NLVINAIPMD FAQPVSFKNA DIGRCVHQKP REDEDGEIPA EVVLPPKPVP TPSRPALTPF
VTHGPCAAES EPALLIGSKQ FGLSKNSHIA IAFDDTKVKN RLTIEFEVRT EAESGLLFYM
ARINHADFAT VQLRNGLPYF SYDLGSGDTN TMIPTKINDG QWHKIKIMRI KQEGIIYVDG
ASNRTVSPKK ADILDVVGIL YVGGLPINYT TRRIGPVTYS IDGCVRNLQM AEAPADLEQP
TSSFHVGTCF ASAQKGTYFD GTGFAKAVDG FKVGLDLLIE FEFRTTRTTG VLLGISSQKM
DGMGIEMIEE KLMVHVNNGA GRFTAVYDAG LPGLLCDGQW HKVRANKLKH RIELTVDGNQ
VEAQSPNQAS TSADTNDPVF IGGFPAGLKQ FGLTTNVRFR GCIRSLRLTK GTGKPLEVNF
AKALELTGVQ PVSCPVN
//
