ID   Q7TQ11_RAT              Unreviewed;       490 AA.
AC   Q7TQ11;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   SubName: Full=Aa1018 {ECO:0000313|EMBL:AAP85374.1};
DE   SubName: Full=Vitronectin {ECO:0000313|Ensembl:ENSRNOP00000046415.5};
GN   Name=Vtn {ECO:0000313|Ensembl:ENSRNOP00000046415.5,
GN   ECO:0000313|RGD:3967};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAP85374.1};
RN   [1] {ECO:0000313|EMBL:AAP85374.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000046415.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046415.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000046415.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046415.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AY318963; AAP85374.1; -; mRNA.
DR   STRING; 10116.ENSRNOP00000075508; -.
DR   Ensembl; ENSRNOT00000039954.6; ENSRNOP00000046415.5; ENSRNOG00000010031.8.
DR   AGR; RGD:3967; -.
DR   RGD; 3967; Vtn.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00530000063751; -.
DR   HOGENOM; CLU_046227_0_0_1; -.
DR   OMA; LGTYNYD; -.
DR   TreeFam; TF332780; -.
DR   Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-RNO-216083; Integrin cell surface interactions.
DR   Reactome; R-RNO-3000170; Syndecan interactions.
DR   Reactome; R-RNO-3000178; ECM proteoglycans.
DR   Reactome; R-RNO-977606; Regulation of Complement cascade.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000010031; Expressed in liver and 18 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:RGD.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR   GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005796; C:Golgi lumen; IDA:RGD.
DR   GO; GO:1904090; C:peptidase inhibitor complex; ISO:RGD.
DR   GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0048237; C:rough endoplasmic reticulum lumen; IDA:RGD.
DR   GO; GO:0005518; F:collagen binding; IDA:RGD.
DR   GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR   GO; GO:0008201; F:heparin binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; ISO:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0097421; P:liver regeneration; IDA:RGD.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:RGD.
DR   GO; GO:0051258; P:protein polymerization; IDA:RGD.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR   GO; GO:0061302; P:smooth muscle cell-matrix adhesion; ISO:RGD.
DR   CDD; cd00094; HX; 1.
DR   Gene3D; 4.10.410.20; -; 1.
DR   Gene3D; 2.110.10.10; Hemopexin-like domain; 2.
DR   InterPro; IPR000585; Hemopexin-like_dom.
DR   InterPro; IPR036375; Hemopexin-like_dom_sf.
DR   InterPro; IPR018487; Hemopexin-like_repeat.
DR   InterPro; IPR018486; Hemopexin_CS.
DR   InterPro; IPR020436; SMB_chordata.
DR   InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR   InterPro; IPR001212; Somatomedin_B_dom.
DR   PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22917:SF3; VITRONECTIN; 1.
DR   Pfam; PF00045; Hemopexin; 3.
DR   Pfam; PF01033; Somatomedin_B; 1.
DR   PRINTS; PR00022; SOMATOMEDINB.
DR   SMART; SM00120; HX; 4.
DR   SMART; SM00201; SO; 1.
DR   SUPFAM; SSF50923; Hemopexin-like domain; 1.
DR   SUPFAM; SSF90188; Somatomedin B domain; 1.
DR   PROSITE; PS00024; HEMOPEXIN; 2.
DR   PROSITE; PS51642; HEMOPEXIN_2; 3.
DR   PROSITE; PS00524; SMB_1; 1.
DR   PROSITE; PS50958; SMB_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q7TQ11};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..490
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014106987"
FT   DOMAIN          20..63
FT                   /note="SMB"
FT                   /evidence="ECO:0000259|PROSITE:PS50958"
FT   REPEAT          156..209
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          210..257
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          428..485
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REGION          80..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..406
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  55960 MW;  0FCBCB6FF5C4E499 CRC64;
     MASLRPFFIL ALLALVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC CVDYMEQCKP
     QVTRGDVFTM PEDEYWSYDY PEETKNSTST GVQSENTSLH FNLKPRAEET IKPTTPDPQE
     QSNTQEPEVG QQGVAPRPDT TDEGTSEFPE EELCSGKPFD AFTDLKNGSL FAFRGDSVDR
     FDGGEYCYEL DETAVRPGYP KLIQDVWGIE GPIDAAFTRI NCQGKTYLFK GSQYWRFEDG
     VLDPDYPRNI SEGFSGIPDN VDAALALPAH SYSGRERVYF FKGTQGKQYW EYEFQQQPSQ
     EECEGSSLSA VFEHFALLQR DSWENIFELL FWGRSSDGAK GPQFISRDWH GVPGKVDAAM
     AGRIYITGST FRSVQAKKQK SGRRSRKRYR SRRGRGHSRS RSRSMSSRRP SRSVWFSLLS
     SEESGLGTYN YDYDMNWRIP ATCEPIQSVY FFSGDKYYRV NLRTRRVDSV NPPYPRSIAQ
     YWLGCPTSEK
//