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Database: UniProt
Entry: A0A2I0MVN3_COLLI
LinkDB: A0A2I0MVN3_COLLI
Original site: A0A2I0MVN3_COLLI 
ID   A0A2I0MVN3_COLLI        Unreviewed;      1433 AA.
AC   A0A2I0MVN3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Laminin, alpha 2 {ECO:0000313|EMBL:PKK33736.1};
GN   Name=LAMA2 {ECO:0000313|EMBL:PKK33736.1};
GN   ORFNames=A306_00000763 {ECO:0000313|EMBL:PKK33736.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK33736.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK33736.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK33736.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
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:PKK33736.1}.
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DR   EMBL; AKCR02000002; PKK33736.1; -; Genomic_DNA.
DR   STRING; 8932.A0A2I0MVN3; -.
DR   InParanoid; A0A2I0MVN3; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0005102; F:signaling receptor binding; 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   Gene3D; 2.10.25.10; Laminin; 13.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF436; -; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 3.
DR   Pfam; PF00053; Laminin_EGF; 16.
DR   Pfam; PF06008; Laminin_I; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00180; EGF_Lam; 15.
DR   SMART; SM00281; LamB; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 11.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 11.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
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   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:UP000053872};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022869};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..32
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          33..81
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          102..287
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          321..370
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          371..428
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          429..481
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          482..530
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          620..666
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          667..712
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          713..818
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          833..1067
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1108..1156
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1215..1261
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DISULFID        8..17
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        52..61
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        340..349
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        399..408
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        453..462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        465..479
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        482..494
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        484..501
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        503..512
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        620..632
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        640..649
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        685..694
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        713..725
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        789..798
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1127..1136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1215..1227
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1217..1234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1236..1245
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1433 AA;  157166 MW;  5EFADD38A18A1B9C CRC64;
     MLPGFCHCKT GYAGESCNRC ALGYTGYPEC LPCNCSLEGS VNVDPCVGPC TCKEHVEGEN
     CDRCKPGFFN LQQKNPKGCE ECFCSGKTNV CTHSHLTYST IEDMNGWYLT GLPGLIRVVP
     KQKQFDGHQQ LSISNVAARK VLPQTYYWSA PSSYLGNKVA AAGGHLKFTV SYDFTEEEET
     VQLIVQSDVI IEGGDLRIST PKEGIHLQPS EEHTEEIVLK PESFSVHGTD LPVSRREFMT
     VLANVKRILI RATYSNGMNA IYRLRSCSIE AADHTSTGRK VASAVELCDC PPGYDGTSCE
     SCWPRHRRVN GTIFGGVCAP CTCFGHAESC DDITGECLDC QHNTGGSYCD RCLPGFYGDP
     TKGTAEDCQL CACPLNIPSN NFSPTCHFDR SRGLICDECP AGYVGPRCER CAEGYFGQPL
     IPGGSCQPCP CNDNLDFSIP GSCDSLSGAC LICKPGTTGQ YCEKCADGYF GDALDARNCQ
     PCHCHINGSF SEICDSRTGQ CECKANVIGR RCGVCKPSYF WAPEKLFCIP CGCSAVGSMS
     LRCDMSGRCI CKSGFVGRRC EISRQMPKLK ENARSSSQQI RVPPRRWGVS SASGCPRGAY
     RPATPPETFG LQSSRGCVPC NCNSFGSKSF DCDGDGQCYC QPGVTGKKCD RCAHGFYNFE
     EGGCTPCECS RFGDNCDPIS GRCICPPNTV GEMCDKCAPN YWGHDIVTGC KPCDCSLIGA
     LSSQCDLNTG CCFCRPEFSG DKCTECRLGY WNYPQCVACQ CFLAGTDPQS CETELGRCSC
     VDHTGQCSCK VNVEGVHCDR CKSGTFSLSA RNPLGCSSCY CFGLTTQCSE ARGLVRTWVT
     LKPEQMILPL VDEKLQRSTL SGIAFQPPEI LANIEQVIQD LRSEPVYWRL PEQFEGRKLT
     AYGGKLKYAI YFEAREETGF TTYYPQVIIR GGPPTHPRII VRHMAAPLIG QLTRHEIEMT
     EHEWGYYGDD QRVRNTVPWE YYHDDPSVNR TVAQADFTWK YYGDDSRPSR PVSREDFLNV
     LYDVHYILIK ATHGNIMRQS RISEISMEVA ESGTVSGVTP QAHLIEKCDC PLGYSGLSCE
     SCSPGFYRLS TSPGGRTPAQ SLGVCVLCQC HGHSTMCDPE TSICQNCQHN TAGHHCERCA
     LGFYGVVQGS PDDCQPCACP LSNPSNNFSP SCVAEGPSDY RCTACPPGYE GQYCERCSSG
     YTGNPQVPGG SCQECECDRY GSLPVPCDPV TGQCTCKPGF TGWKCAGCEH RHARDGMRCI
     SCDDECTGLL LSDLDRLNQM ILSVNLSGPL PAPYKMLHGF ENVTQELKHL LSPQQAPERL
     LQLAQENLDT LVTEMDELLT RATKVTADGE QTRQDAERTN DRAKSLGQFV KGILQAAEAA
     NEDAIKLNET FRTQDETLEK SLPELQSEAD RMIAEMRSRE LNMQERIAQD ELK
//
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