ID A0A3Q4M2R1_NEOBR Unreviewed; 2897 AA.
AC A0A3Q4M2R1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Laminin subunit alpha-2-like {ECO:0000313|Ensembl:ENSNBRP00000001064.1};
GN Name=LAMA2 {ECO:0000313|Ensembl:ENSNBRP00000001064.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000001064.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000001064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 32507.ENSNBRP00000001064; -.
DR Ensembl; ENSNBRT00000001117.1; ENSNBRP00000001064.1; ENSNBRG00000000411.1.
DR GeneTree; ENSGT00940000155362; -.
DR OMA; GMPEDCQ; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000000411; Expressed in muscle tissue and 4 other cell types or tissues.
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:0048856; P:anatomical structure development; IEA:UniProt.
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; 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; 13.
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; IPR008979; Galactose-bd-like_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; 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; 15.
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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 11.
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:UP000261580};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2897
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018656186"
FT DOMAIN 9..255
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 383..437
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 438..486
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 507..670
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 704..753
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 754..811
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 812..864
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 865..913
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 914..960
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 961..1006
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1007..1052
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1053..1112
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1097..1277
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1278..1341
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1928..2111
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2121..2300
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2305..2498
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2536..2709
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2714..2892
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2496..2541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1579..1625
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1735..1762
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1840..1923
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2512..2526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 383..395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 413..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 457..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 723..732
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 782..791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 836..845
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 848..862
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 865..877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 867..884
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 886..895
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 914..926
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 934..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 979..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1007..1019
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1009..1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1028..1037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1053..1065
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1083..1092
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1312..1321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2471..2498
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 2897 AA; 318626 MW; E4F853205F0B49C7 CRC64;
MSVFFLFFSS PGLFPAVLNL ATMANITTNA TCGSTGPEMF CKLVEHVPGQ PVRNAQCQIC
NQRKHHPIEY AIDGTNRWWQ SPSIKNGMEY HYVTITLDLK QVFQIAYVII KAANSPRPGN
WILERSIDGV TFEPWQYYAI TDTECLTRFN INPRTGPPSY TRDDEVICTS FYSKIHPLEN
GEIHTSLING RPSADDPSPT LLNFTSARYI RLVFQRIRTL NADLMTLTLH DPKDMDPIVT
RRYYYTIKDI SVGGMCICFG HAKACPLNSV TKKFSCECEH NTCGESCDRC CPGYHQQPWM
AGTFLTRHVC EKCNCHGKAE ECYFNQTVAD LSLSQDIHGQ YKGGGVCIGC RDDTAGINCQ
SCVPGFYRPA DVSAEEESPC IPCSCDPYGS ISQTCVADSS QATPRQPAGS CWCKEGFWGL
RCDRCAIGYT GYPYCERCNC SVEGSVNADP CITPCICKEN VEGENCDRCK LGFYNLQESN
RRGCEKCSCM GVSSQCTAST WTYQNETTLT GWHLVGNTGG RVWSVHRETP PYLSVRHLDV
VDDLGTAYYW NAPGLYLGNK VMSIRVTSEP DLIIEVRGMK INYKRFGEPV YPSSSSTSHI
VLLPENFRVS ETAQPVSRRD FLSVLAKVTS VMVRASYSTE RSAVYRLHSF SMEVANPAAR
GERRASAVEV CSCPYGYGGT SCEACVLGFR RVNGNLYNGV CEPCHCHGHT TQCHEVTGHC
LDCSHSTAGP YCDTCLPGYY GNATRGSPAD CQPCACPLNI PSNNFSPTCH LSQDGELLCD
QCRPGYTGPR CDRCSNGYYG QPTVPGGSCR LCDCNGNLDL SIPGSCDPNT GRCLRCRQGY
GGEACDSCAA SYYGDAIIAK DCQPCQCHTN GSVSEVCNQE TGECHCKENV LGQKCDKCRA
GTHGLTTGGA CIPCHCNSYG SKSFDCDENG QCRCQPGVTG PKCDRCSRGY FNFQEGGCTP
CQCSHVGNNC DANTGQCICP PNTIGERCDR CAPNHWGHDI VTGCKECGCN VIGSVTQQCN
VNTGCCNCHD SFRGDKCNEC QIGYRDFPQC VQCKCNIAGS DRQTCDQERG ACGCADRTGK
CSCKENVEGD YCDHCKPDTF GLSLRNPLGC SRCYCYGLTH FCTEAQGLIR MWVSKPVFYF
VPKNFLKNKI TAYGGQLKYA VYYEAREETG PSSYEPQVII KGGPNHNMVM TRHITGLQIG
QLTRHEIDMT EHDWKFADGR TMTREDFMDI LFYVDYILIK ASHGNLMRQS RISEISLTVA
EEGRPTKESE KAHQIEKCDC PIGYSGLSCE KKPPSAHKNK KSPLPVGRWP NCQDNTEGDR
CERCAPGFYG VVRGSPDDCK PCAYCMLQIP TCVAEGFDDY RCTACPEGYE GKHCERCATG
YHGNPRIPGG HCEECKCSLW GALPGPCDPV TGQCRCRVGA SGMTCDQCMD RHVCGPSGII
SCDDECSGLL ISDMDRLLRI INEVTLTTPL PPPYKVLYRF ENMTEELKHM LSPQKAPERL
LQLADSNLGS LVTEMDQLHS RATKVSADGE QVEDDADRIH KRAEDLEQFI RDTLLGAKDL
ESKAAELNQS LSRRGGTPEK SLSEMKEEIQ AMLHEMRQRR LGGKKVIAEE ENNLAEELYQ
KVQRLFGKPH QATEDLKAEV TINFTYLSSV LLNEWLNTSL SDLEEMASEL GALHGRLDDR
VSHLTYGLSD GRLAYRVQDA EEHARQLNDS AAILDGILAE AKNLSFNATA AFNAYSNIKA
NVDAAEKEAK AAKQRASEAL ALVRGRALPC METHAVSGVA GLKGRVKAAK DKTKDLLKAV
NGTMATLNAI PNGMIASLLA ATKAVAADAN ATAIDVLERL GDLNLRLGGL ERNYTDLKET
VSEANQMIQD PEKNIHAAGA KVKDLEDEAD RLLEKLQPIK KLQDNLRRNI SQIKELINQA
RKQANSIKVS VSSGGDCLRS YRPDIRKGRY NTIILHVKTT TPDNLLFYLG SAKYVDFLAL
EMRKGKVNFL WDVGSGVGRV EYPHHTIHDG NWHRIEASRN GLNGTISVYP LEGSMAGMMP
TPASANSPTA FTILDVDQNA YLFVGGIFGS VKKAETVRTN TFTGCMGETY LDGKPIGLWN
YREREGDCKG CVVSPQRSHG EGTVQLDGEG YAAVGRPTRW NPNVSTITFK FRTFSSDALL
MYMAAEDMKD FMSLELSEGK VKVNFDLGSG VGSANSSKRH NDGHWKSLTM SRNKKLSTVS
IVDVDSSDEE KIVATSLGSA TGLNLKEHQK IYFGGLPTIG NYRSEVILKR YAGCLRDIEI
SRTPYNLLSS SDYTGVTKGC NVENLHTVSF SKPGYMELSG LSLAVDTEIS LSFSTLEDTG
TILLAVGRGW TQVTHLSNSI TQVIYLQLWQ PYLSVMLTRG SLEVVVSTGS HNRRQATRRP
EQGTLNDGRE HTLRIERLAG RSFAVHVDDE ARMQGVLPND QPLNLQRIFL GGIPAEVEQT
SNRANIPFKG CIWNLMINAV LSDFAQSVSF ENAEIGQCPN LAPPPPPPPL PAEKELEKEK
EDSKPSTPIS PRPSPPADVT TIKNSHMSFA FDDNNVRDKL KIEFELRTKE SSGLIFYMAR
INHADFVSIQ IKNGQVCLGY DLGHGNISDC VPYSINDGSW HKISVTRDRQ RATLIVNRRF
QKMMSSPKKA DLLDVVGILY IGGLPQNYTT KRIGPILYSI NGCIRSSESM IDFKLDMATP
TSSHMVGRCF VATETGTYFE GTGFLKAVSS YRVGLDVSIA LEFRTSRTSG VLLAVSNQGN
DGLGLEIVDG KLLFHVDNGA GRFTAVHVPQ GEGFCDGQWH SITATKKRNK LELVVDGKQS
DAASLYAHSV TCDTSDPIYV GGYPAGVHQA ALSTSTSFHG CIRNLKITKS SKTMEVHFNK
ALEIRGVQPL SCPAVAA
//
