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Database: UniProt
Entry: A0A2K6D5S1_MACNE
LinkDB: A0A2K6D5S1_MACNE
Original site: A0A2K6D5S1_MACNE 
ID   A0A2K6D5S1_MACNE        Unreviewed;      3324 AA.
AC   A0A2K6D5S1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Laminin subunit alpha 3 {ECO:0000313|Ensembl:ENSMNEP00000031250.1};
GN   Name=LAMA3 {ECO:0000313|Ensembl:ENSMNEP00000031250.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000031250.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000031250.1}
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   Ensembl; ENSMNET00000055674.1; ENSMNEP00000031250.1; ENSMNEG00000038755.1.
DR   GeneTree; ENSGT00940000155638; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000038755; Expressed in colon and 11 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: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; 13.
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; 11.
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:SF285; LAMININ SUBUNIT ALPHA-3; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF02210; Laminin_G_2; 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; 7.
DR   SMART; SM00180; EGF_Lam; 13.
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; 11.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 8.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
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:UP000233120};
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..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..3324
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014399336"
FT   DOMAIN          43..298
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          426..469
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          491..535
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          536..588
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          631..683
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1266..1311
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1356..1404
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1405..1455
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1476..1653
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1687..1733
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2381..2582
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2589..2751
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2758..2918
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2977..3141
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          3148..3321
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          1844..1906
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2012..2053
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2089..2160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2316..2374
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        445..454
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        491..503
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        511..520
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        536..548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        538..555
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        557..566
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        654..663
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1266..1278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1268..1285
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1287..1296
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1380..1389
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1405..1417
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1407..1424
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1426..1435
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1706..1715
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   3324 AA;  365837 MW;  EE2E53A0953BD003 CRC64;
     MAAAARPRGR APGPVLPPTP LLLLVLQLLP AWGATARDPR AAAGLSLHPP YFNLAEAARI
     WATATCGERG PSERRPRPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI
     DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST
     YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA
     KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGRCV
     CNGHAEVCNA NNPEKLFRCQ CQHHTCGETC DRCCTGYNQR RWQPAAWEQS HECEACNCHG
     HASDCYYDSD VERQQASLNT QSIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP
     DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAVG YYNFPFCLKI PIFPVSTPSP
     EDPVAGDIRG CDCNPEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACLCSA
     LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TIDSNLGSCP
     CKLHVEGPTC SICKPLYWNL DKENPNGCSE CQCHKAGTVS GTGECRQGDG DCHCKSHVGG
     DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSVCSGPS GVCQCREHVV GKACQRPENN
     YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPGFSWRG YAQMTSVQND VRITLNVGKS
     SGSLFHVILR YINPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS
     ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT
     RFPCTLACEA RRFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRV PQVGRYVVVL
     EYSTEAAQLF VADVNVKSPG SVLAGQVNIY SCKYSVLCRS AVIDHMSRIA VYELLADADI
     QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYRRF VNQSATCVSL AHETPPTALI
     LDVVSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR APHLGRYVFV IHFYQAAHPT
     FPAQVSVDGG WPRAGSFRAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV
     LVRVLMVPTE NYDYQILHKK SMDKSLEFIT NCGKNSFYID PQTASRFCKN SARSLVAFYH
     KGALPCECHP AGATSPHCSP EGGQCPCRPN VIGRQCTRCA TGHYGFPHCK PCSCGLRLCE
     EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTSEAAMLQ CDRDSGQCRC
     KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE
     GSFHLDPANP KGCTSCFCFG VNNQCHSAHK RRAKFVDMLG WCLETADRMH IPVSFNPGSN
     SVVADLQELP ATVHSASWVA PASYLGDKVS SYGGYLTYQA KSFGLPSDMV LLEKKPDVQL
     TGQHMSVIYE ETNTPRPDRL HHGRVQVVEG NFRHASSRAP VSREELMTVL SRLADMRIQG
     LYFTETQRLT LSEVGLEEAS DTGSGRIAYA VEMCACPPAY AGDSCQGCSP GYYRDHKGLY
     TGRCVPCNCN GHSNRCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN
     RFATGCVVNG GDVRCSCKAG YTGTQCCMEN PFLKCSLCIG LSFFQNPHPS LRRPGPTAPP
     ASHLPLIVAP TDCDSCVMTL LNDLATMGEQ LRLVKSQLQG LSASAGLLEQ MRHMETQAKD
     LRNQLLNYRS TISNHGSKIE GLERELTDLN QEFETLQEKA QVNSRKAQTL YNNVNRAIQS
     AKELDMKIKT VIRNVHILLK QISGPDGEGN NVPSGGFSRE WAEAQRMMRE LRNRNFGKHL
     REAEADKRES QLLLNRIRTW QKTHQGENNG LANSIRDSLN EYEAKLSDLR ARLQEAAARA
     KQANGLNQEN ERALGAIQRQ VKEINSLQSD FTKYLTSADS SLLQTNIALQ LMEKSQKEYE
     KLAASLNEAR QELSDKVREL SRSAGKTSLV EEAEKHAQSL QELAKQLEEI KRNASGDELV
     RCAVDAATAY ENILNAIKAA EDAANRAASA SESALQTVIK EDLPRKAKTL SSNSDKLLNE
     AKMTQKKLKQ EVSPALSNLQ QTLNIVTVQR EVIATNLTTL RDGLRGIQRG DIDAMISSAK
     SMVRKANDIT DEVLDGLNPI QTDVERIKDT YGSTQNEDFK KALTDADNSV NKLTNKLPDL
     WRKIESINQQ LLPLGNISDN MDRIRELIQQ ARDAASKVAV PMRFNGKSGV EVRLPNDLED
     LKGYTSLSLF LQRPNSRENG GTENMFVMYL GNKDASRDYI GMAVVDGQLT CVYNLGDHET
     ELQVDQILTE SETQEAVMDR VKFQRIYQFA RLNYTKGATS SKPEIPGVYD MDGRNSNTLL
     NLDPENVVFY VGGYPPDFKL PSRLRFPPYK GCIELDDLNE NVLSLYNFKK TFNLNTTEVE
     PCRRRKEESD KNYFEGTGYA RVPTQPHASI PTFGQTIQTT VDRGLLFFAE NRDRFISLNI
     EDGKLMVRYK LNSEPPKERG VGDAINNGRD HSIQIKIGKV QKRMWINVDF QNTIIDGEVF
     DFSTYYLGGI PIAIRERFNI STPAFRGCMK NLKKTSGVVR LNDTVGVTKK CSEDWKLVRS
     ASFSRGGQLS FTNLGSPLTD HLQASFGFQT FQPSGILLSH QTRTSTLQVT LEDGHIELST
     RDSGSPIFKS PQTYMDGLLH YVSVISDNSG LRLLIDDQPL RNNQRLNRIS SSQQSLRLGG
     SNFEGCISNV FVQRLSLSPE VLDLASNSLK RDVSLGGCSL NKPPFLMLLQ GSTRFNKAKT
     FRINQLLQDT PVASPRSMKV WQDACSPLPR TQANHGALQF GDIPTSHLLF KLPQELLKPR
     SQFAVDVQTT SSRGLVFHTG TKNSFMALYL SKGRLVFALG TDGKKLRIKS KEKCNDGKWH
     TVVFGHDGEK GRLVVDGLRA REGSLPGNST VSLRGPVYLG SPPSGKPKSL PTNSFVGCLK
     NFQLDSKPLD TPSSSFGVSS CLGGPLEKGI YFSEEGGHVI LAHSVLLGPE FKLVFSIRPR
     SLTGILIHIG SQPGKHLGVY LEAGKVTASM DSGAGGTSTS VTPKQSLCDG QWHSVAVTIK
     QHILHLELDT DSSYTAGQIP FPPASTQEPL HLGGAPANLT TLRIPVWKSF FGCLRNIFVN
     HIPVPVTEAL EVQGPVSLNG CPDH
//
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