ID A0A091MKD2_CARIC Unreviewed; 1727 AA.
AC A0A091MKD2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Laminin subunit alpha-3 {ECO:0000313|EMBL:KFP62020.1};
DE Flags: Fragment;
GN ORFNames=N322_09778 {ECO:0000313|EMBL:KFP62020.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP62020.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP62020.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP62020.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK507961; KFP62020.1; -; Genomic_DNA.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00055; EGF_Lam; 12.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
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; 1.
DR Pfam; PF00053; Laminin_EGF; 14.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 14.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 12.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Secreted {ECO:0000256|ARBA:ARBA00022869}.
FT DOMAIN 1..203
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 333..376
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 403..447
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 448..492
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 496..541
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 542..594
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1188..1233
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1278..1326
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1327..1377
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1398..1577
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1611..1657
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1658..1710
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 352..361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 403..415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 423..432
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 448..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 468..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 512..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 565..574
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1188..1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1190..1207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1209..1218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1302..1311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1327..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1329..1346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1348..1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1630..1639
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1658..1670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1681..1690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP62020.1"
FT NON_TER 1727
FT /evidence="ECO:0000313|EMBL:KFP62020.1"
SQ SEQUENCE 1727 AA; 190932 MW; 7AF6C1B1504894E6 CRC64;
AFQGQFCDYC NAADPSKAHP VTNAIDGTER WWQSPPLSMG LKYNEVNVTL DLGQLFQVAY
ILIKFANSPR PDLWILERSV DFGRTYTPWQ YFAHSKADCF ERFGKEANLP VRRDSDVLCT
TEYSRILPLE NGEIVVSLVN GRPGAKNFTY SPSLREFTKA TNIRLHFLRT NTLLGHLISK
AQRDPTVTRR YYYSIKDISI GGRCVCHGHA EVCNAESVEN QYQFQCECQH NTCGETCDHC
CPGYNQKQWQ PATAGSTNIC EPCNCHGHAT DCYYDPDVDQ RQESLNIHGH YEGGGVCINC
QHNTAGINCE KCAKGYYRPY GVPARAPDGC IPCSCNSEHA EGCEEGSGRC FCKQNFQGEN
CERCADGFYG YPFCVYTSVY PFTSPNPRDA MAGDIIGKFL FLCECNLAGT QPEICDFLGR
CLCRAGVTGL QCDDCHPGHH SFPACQECNC DAVGSVENTC DPRGQCLCHS NYAGLRCDQC
APGYYGYPSC LRVNSECDPS GSVGSHSGYC QCLQHVEGPT CSKCKPLYWN LAKENPEGCT
ACQCDMSGTL SGVGECQQEN GHCYCKANVC GDSCDTCEAG YYALENKNYF GCRGCLCDVG
GSLSPACAEP WGGCRCRAHV VGTACQEPEK NYFFPDLHHM KFEIEDGTTV KGREIRFGYD
PQEFPSFSWR GYARMSSIQN EVRITLNVEK SNLYLFRIIL RYINPGGETL SGRISAWQSR
PETGAAQSKE FVFPPSKEPA FVTIPGKSST EPFTLVPGTW TVSIMAEEVL LDYMVLLPSD
YYEASILQIQ VTEPCTYSGR ASTEHCLLYQ HLPLGRFSCV LGSEAAYFRH GGEYRRIPVR
QPTPDQPVMT HISGREVNLQ MTINVPQVGR YVLVFEYANE EDQLYTAEVI IHSPGPVTEG
RVRIYSCKYS FLCRSIVVDN RNRIAAYDLL ADTKIHLKAS SINFLLHKVC IIPAEEFSPE
YVDPKVQCIA AYRSTRDRSA TCIPSVYETP PAALVLDAFK DGKISEVRRN ILDDPLSAPL
PSDSVNGVTL SPLQNQITLS GRVPRLGRYV FVVHFYQPAH LVFPVQVQVD GGHVWSGSFN
ASFCPHTSGC RDQVIAENQI ELDISEPEVS VTVMIPDGRI LVLENILVVP ADTYSYKILD
KKTVDKSFDF ISQCGGNSFY IDPEGSSTFC KNSARSLVAF YNNGALPCNC HSAGATSPTC
SPLGGQCICR PNVIGRQCSR CQTGYYGFPF CKLCNCGQRL CDDMTGKCIC PPRTVKPTCE
VCERHYFSYH PLAGCESCNC SERGVVNAAS PECEKTNGQC KCKPGIKGRQ CDHCAPGTYG
FPNCMPCNCN RDGTEPDVCD PQTGICLCKE NVEGAECDTC RPGSFYLDPS NPRGCTSCFC
FGATSDCRST NRRRTKFVDM RDWRLEAVDD NIDIPVTFNP VSNSVVADVQ ELPASVHGLY
WKAPPSYLGE KLSSYGGFLS YQVKSFGLPS EGMVLLDKRP DIQLTGQHMK VVYMDPNNPL
PDRQYYGRVQ LVEGNFRHAS SNNLVSREEL MIILSRLDGL HIRGLYFTET QRLTLGEVGL
EEATSAGSSS IAYSVETCSC PPEYTGDSCQ ECGLGFYREN KGLFTGRCVP CNCNGNSNRC
QDGTGRCINC QYNTAGEKCE RCKDGYFGDA TQGSCRVCPC PYTNRFATGC VANGEEIQCL
CKEGYTGVRC ERCAPGYFGN PQKYGGYCQK CNCNNNGQLA SCDHLTG
//
