ID   B1AHL2_HUMAN            Unreviewed;       721 AA.
AC   B1AHL2; C9JMQ3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   16-JAN-2019, entry version 83.
DE   RecName: Full=Fibulin-1 {ECO:0000256|PIRNR:PIRNR036313};
GN   Name=FBLN1 {ECO:0000313|Ensembl:ENSP00000385521};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000385521, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000385521, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [2] {ECO:0000313|Ensembl:ENSP00000385521}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers.
CC       May play a role in cell adhesion and migration along protein
CC       fibers within the extracellular matrix (ECM). Could be important
CC       for certain developmental processes and contribute to the
CC       supramolecular organization of ECM architecture, in particular to
CC       those of basement membranes. {ECO:0000256|PIRNR:PIRNR036313}.
CC   -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC       matrix components. {ECO:0000256|PIRNR:PIRNR036313}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|PIRNR:PIRNR036313}.
CC   -!- SIMILARITY: Belongs to the fibulin family.
CC       {ECO:0000256|PIRNR:PIRNR036313}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; AL021391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z95331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z98047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; B1AHL2; -.
DR   EPD; B1AHL2; -.
DR   jPOST; B1AHL2; -.
DR   MaxQB; B1AHL2; -.
DR   PeptideAtlas; B1AHL2; -.
DR   PRIDE; B1AHL2; -.
DR   Ensembl; ENST00000402984; ENSP00000385521; ENSG00000077942.
DR   UCSC; uc010gzz.4; human.
DR   EuPathDB; HostDB:ENSG00000077942.18; -.
DR   HGNC; HGNC:3600; FBLN1.
DR   OpenTargets; ENSG00000077942; -.
DR   GeneTree; ENSGT00940000156642; -.
DR   HOGENOM; HOG000007079; -.
DR   PhylomeDB; B1AHL2; -.
DR   ChiTaRS; FBLN1; human.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000077942; Expressed in 217 organ(s), highest expression level in endocervix.
DR   ExpressionAtlas; B1AHL2; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR   CDD; cd00017; ANATO; 1.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR017048; Fibulin-1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   Pfam; PF12662; cEGF; 3.
DR   Pfam; PF07645; EGF_CA; 4.
DR   PIRSF; PIRSF036313; Fibulin-1; 2.
DR   SMART; SM00104; ANATO; 3.
DR   SMART; SM00181; EGF; 9.
DR   SMART; SM00179; EGF_CA; 8.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 3.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|SAAS:SAAS00909960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00601599};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00032677};
KW   Extracellular matrix {ECO:0000256|PIRNR:PIRNR036313};
KW   Proteomics identification {ECO:0000213|EPD:B1AHL2,
KW   ECO:0000213|MaxQB:B1AHL2, ECO:0000213|PeptideAtlas:B1AHL2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|SAAS:SAAS00594563};
KW   Secreted {ECO:0000256|PIRNR:PIRNR036313};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30    721       Fibulin-1. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002759898.
FT   DOMAIN      115    148       Anaphylatoxin-like.
FT                                {ECO:0000259|PROSITE:PS01178}.
FT   DOMAIN      150    182       Anaphylatoxin-like.
FT                                {ECO:0000259|PROSITE:PS01178}.
FT   DOMAIN      346    380       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      394    436       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      437    478       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      479    518       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      519    562       EGF-like. {ECO:0000259|PROSITE:PS50026}.
SQ   SEQUENCE   721 AA;  78329 MW;  B65CBC82102501D5 CRC64;
     MERAAPSRRV PLPLLLLGGL ALLAAGVDAD VLLEACCADG HRMATHQKDC SLPYATESKE
     CRAVGLASLC QDLNGAWAVW KVGRASQAEG TASARAQRRG MVQEQCCHSQ LEELHCATGI
     SLANEQDRCA TPHGDNASLE ATFVKRCCHC CLLGRAAQAQ GQSCEYSLMV GYQCGQVFQA
     CCVKSQETGD LDVGGLQETD KIIEVEEEQE DPYLNDRCRG GGPCKQQCRD TGDEVVCSCF
     VGYQLLSDGV SCEDVNECIT GSHSCRLGES CINTVGSFRC QRDSSCGTGY ELTEDNSCKD
     IDECESGIHN CLPDFICQNT LGSFRCRPKL QCKSGFIQDA LGNCIDINEC LSISAPCPIG
     HTCINTEGSY TCQKNVPNCG RGYHLNEEGT RCVDVDECAP PAEPCGKGHR CVNSPGSFRC
     ECKTGYYFDG ISRMCVDVNE CQRYPGRLCG HKCENTLGSY LCSCSVGFRL SVDGRSCEDI
     NECSSSPCSQ ECANVYGSYQ CYCRRGYQLS DVDGVTCEDI DECALPTGGH ICSYRCINIP
     GSFQCSCPSS GYRLAPNGRN CQDIDECVTG IHNCSINETC FNIQGGFRCL AFECPENYRR
     SAATRCERLP CHENRECSKL PLRITYYHLS FPTNIQAPAV VFRMGPSSAV PGDSMQLAIT
     GGNEEGFFTT RKVSPHSGVV ALTKPVPEPR DLLLTVKMDL SRHGTVSSFV AKLFIFVSAE
     L
//