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Database: UniProt
Entry: U3JUZ9_FICAL
LinkDB: U3JUZ9_FICAL
Original site: U3JUZ9_FICAL 
ID   U3JUZ9_FICAL            Unreviewed;      3039 AA.
AC   U3JUZ9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000006603};
GN   Name=LAMA1 {ECO:0000313|Ensembl:ENSFALP00000006603};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae;
OC   Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006603, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000006603}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2013) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR   EMBL; AGTO01020496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59894.ENSFALP00000006603; -.
DR   Ensembl; ENSFALT00000006632; ENSFALP00000006603; ENSFALG00000006330.
DR   GeneTree; ENSGT00940000157124; -.
DR   OMA; NPKERHP; -.
DR   Proteomes; UP000016665; Unplaced.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005606; C:laminin-1 complex; IEA:Ensembl.
DR   GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR   GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR   GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
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   GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR   Gene3D; 2.60.120.1490; -; 1.
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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 17.
DR   Pfam; PF00054; Laminin_G_1; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00180; EGF_Lam; 17.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016665};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00122,
KW   ECO:0000256|SAAS:SAAS00814887};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00580772};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Repeat {ECO:0000256|SAAS:SAAS00814929}.
FT   DOMAIN        1    222       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      223    279       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      280    349       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      350    406       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      407    455       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      476    661       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN      695    743       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      744    801       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      802    854       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      855    903       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      904    950       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      951    996       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      997   1042       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1043   1102       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1130   1314       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1356   1404       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1405   1461       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1462   1508       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     2075   2255       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2263   2439       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2444   2630       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2677   2849       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   DOMAIN     2854   3034       LAM_G_DOMAIN. {ECO:0000259|PROSITE:
FT                                PS50025}.
FT   COILED     1927   1947       {ECO:0000256|SAM:Coils}.
FT   COILED     2015   2042       {ECO:0000256|SAM:Coils}.
FT   COILED     2046   2070       {ECO:0000256|SAM:Coils}.
FT   DISULFID    245    254       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    317    326       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    350    362       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    382    391       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    426    435       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    713    722       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    772    781       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    826    835       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    838    852       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    855    867       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    857    874       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    876    885       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    904    916       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    924    933       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    969    978       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    997   1009       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    999   1016       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1018   1027       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1043   1055       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1073   1082       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1375   1384       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1432   1441       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1462   1474       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1464   1481       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1483   1492       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   2603   2630       {ECO:0000256|PROSITE-ProRule:PRU00122}.
SQ   SEQUENCE   3039 AA;  333822 MW;  4548017F35245F1A CRC64;
     MFCKLVEHVP GRPLRNAQCR VCDRHSANPK EQHPISSAID GTNNWWQSPS IQNGRQYHWV
     TITLDLRQVF QVAYVIIKAA NAPRPGNWIL ERSIDGTEFR PWQYYAISDT ECLTRYNITP
     RIGPPTYKRD DEVICTSYYS RLVPLEHGEI HTSLINGRPS ADDPSQKLLE FTSARYIRLR
     LQRIRTLNAD LMTLSHNDPK ELDPIVTRRY YYSIKDISVG GMCICYGHAR SCPLDEITKK
     LQCQCEHNTC GESCNKCCPG YHQKPWRPGT LSAGNKCEKC NCHNKAEDCY YNQSIADQKR
     SMDIHGQYLG GGVCLNCTQH TTGINCEMCA DGYFRPHKVS PYEDHPCYPC DCDPFGSLSS
     VCVKDEHHSD SQRGTWPGQC QCREGYAGEK CDRCAFGYQG YPNCLRCNCS LVGSINEDPC
     TEPCLCKENV EGENCDLCKP GFYNLQERNP QGCTECFCFG VSDVCDSLTW PVSQISDMTG
     WLVTDLYKAR SVQPQRSQYD GPHQISINNT EAVKVLKNTY YWSAPEAYLG NKLTAFSGEL
     KYTVSYDIPM ESVDSDIVSS VDVIIQGNGQ ILSTRAAGLS LQPYEEYSNS VRFVSENFIE
     FNTKKAIDRE MLMTVLANVT HLLIRANYNI AKKAVYRLDS VTLDTANANV IDLSSAPDVE
     FCECPQGYTG ISCESCLPGY YRVDGILFGG ICQPCKCNGH ATECDIHGVC FACQHNTTGP
     FCDQCLPGFY GNPSQGTSED CQPCACPLSS AANNFSPTCQ LNEEGGIVCD KCLPGYTGSQ
     CERCANGYYG NPLMPGQSCA PCECNGNVNP QEEGHCDPFT GQCLKCLGNT AGHHCEKCAD
     GYYGDAVTDK NCRACACHVN GSLSSTCQHE TGVCSCKSNV IGERCDKCLN GYYGLLTGLG
     CVPCNCSQFG SVSEECNHQG QCHCVPGVAG EKCDRCAHGF YAFQDGGCTP CDCAHTQNNC
     NADSGQCICP PHTQGQKCEL CEENYWGLSP KLGCKACNCS STGSASLQCD VLTGQCQCKT
     EFGGRECSRC ALGYRDYPDC VACDCDLSGT RAETCNDTEG VCGCEEETGI CACKENVFGL
     QCSECKPGTF GLSANNALGC TPCFCFGMST SCSELEDHVR IPITLTPDQA ILHVVAQSNL
     TGTVEGVFSQ FSDVLLDAAI VRKFLNTETF YWKLPEQFQG DQLMAYGGKL RYTVAFYALD
     GFGTSNFEPQ ILMKGGHTSK LVIYVDIPSP ENGVRTEKEV EMKEDSWKYF NSVSDEPVLR
     SDFMSVLSNV EYILIKAAYG QGLQQSRIAN ISMELAVKFE EMHVGRPLAH LVEQCRCPAG
     YTGLSCQSCA PGYYRRKHTE LSVREPHTLI APCVPCQCNN HSETCDPDTG KCLNCRDNTV
     GDYCSACAPG YYGRVTGSAN DCSLCACPRA NSVSFSPTCV LKGVQDYLCD ACLPGYEGQY
     CERCSPGYYG APQLPGGSCR PCQCNPGGSV DGNCDGATGQ CLCKPGVTGQ LCEECEPRHL
     LLEDECVSCD DNCTGVLLNS LDNLQEAMLS VNLTGIDRVP YGILSELENA TQHLKRSVVP
     REDTTYSLDT AEENLLNLSG GIDYLHEETT RFLKQAQQLD TMTQKTRNKS QELTGFIDTV
     HTTIKVLAEV ALSLNETLGL DLPLSNAASQ RLQDDISALL DALRKKDFVR QHHNATTVLK
     AAEKLLTQVQ KEYFKPQQEL AELKTDASQF LSKQNGRLQD VQDLVNEALA DISETHRLFP
     LITSNLAELN DKKLKIKEGE EVSTMLIKEG KVLLNAAAAL AQDVKNSTFN AEVHQDGLVL
     WSTKLRHHVD ELVMQMSVRG VLDLVYRAEE HATQFQRLAD ALESDLSRVR NLTLNATAAI
     DTHSSVKSVI ERTESLADDA SRVMNGPLDL PDESFSLLGK ETLLLSSKFQ NEAKNLKKKN
     DGLLFGLNEL KKKVEKTQES TNKIGNQLND SLLTLRALPN NTRKYMLEVK ELALSANTSA
     VVDLSHFGEF SQKLMNTSAT LSQVNDSLRK TSELITDSSK AASTAEKQVK EVEAQASLLL
     DRLKPLKMLE ENLNRNLSEI KELISQARKQ AASIKVAVSA DRDCIRAYQP QISSTNYNTL
     TLNVKTAEPD NLLFYLGSNG KTDFLAVEMR RGKVALLWDL GSGSTRVEYP DFQIDNNKWH
     RIHATRFGKT GTLSIEEMNS NQKPSPKSGT SPGTASILDV NKSTLMFIGG LGGQIKKSPA
     VKVTHFKGCL GEASLNGKSV GLWNYVEREG KCNGCFGSPQ DEDTSFHFDG SGYSVVEKAL
     RSTVTQIIIF FSTFSPNGLL LYLASNGTRD FLSLELVDGK VRATVDLGSG PLALTTENRY
     NNGTWYKISF NRNKKQGILA VMDAYNLNYK ETKQGESPGV ASDLNRSDKD PVFIGGLPRS
     RALRKGLNSR MYVGCIKNLE ISRSTFDLLR NSYGVRKGCV LEPIHSVSIM NNGYIELVPK
     SLSPESELMA TFATKNSSGI ILAGLSRGLE KRRRRQAHLP FFSIMLIDGH LAVHVNAGDR
     ASSRKVVLQS ANGTYSDGQE HSVILIRNKR IITVQVDESK PAELRLGSAA ENSPINISNF
     YAGGIPAGEG ILGLKLAGSF HGCISNLIFN KELLYFTTSM KYEHVDMDSC FLSEKPKPSD
     IVIQPELQAL PVPLRPLTDT KKVVCAKDEL PDHVQGAHQF GLAKGSHLTL LFNQSAVRKK
     LSIQLTLRTF ASSGLIYYMA HQNQVDYAAL QLYGGQLHFS FDLGKGKAVA LHHAVVSDGK
     WHTVKTEYVK RKGTIIVDGQ ELVEVSALGD GSTLDVEGKL YVGGLPLDYI PKNLGNVTHS
     IPACIGSMTI NGKQLDNESP VSIFAVNKCY ETVQEGTFFD GSGFAALVRE GYKVRSDVNI
     TLEFRTTAVH GVLLGVSSAK VDAIGLEIVH GKVLFHVNNG AGRITVTYEP RGTNSLCDGK
     WHKLQANKSK HRISLIIDGN LVHTDNPYVQ STSADTNNPI YVGGYPADVK QNCLTSKSSF
     RGCLRNLVLT KGQHTELFDF SRAFDLRGVF PHSCPGAEH
//
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