ID   AGGF1_MOUSE             Reviewed;         711 AA.
AC   Q7TN31; Q8R2S6; Q9CQR9; Q9CU87; Q9D768;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Angiogenic factor with G patch and FHA domains 1;
DE   AltName: Full=Angiogenic factor VG5Q;
DE            Short=mVG5Q;
GN   Name=Aggf1; Synonyms=Vg5q;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14961121; DOI=10.1038/nature02320;
RA   Tian X.-L., Kadaba R., You S.-A., Liu M., Timur A.A., Yang L., Chen Q.,
RA   Szafranski P., Rao S., Wu L., Housman D.E., DiCorleto P.E., Driscoll D.J.,
RA   Borrow J., Wang Q.;
RT   "Identification of an angiogenic factor that when mutated causes
RT   susceptibility to Klippel-Trenaunay syndrome.";
RL   Nature 427:640-645(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Small intestine, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Promotes angiogenesis and the proliferation of endothelial
CC       cells. Able to bind to endothelial cells and promote cell
CC       proliferation, suggesting that it may act in an autocrine fashion (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the secreted angiogenic factor TNFSF12.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}.
CC       Note=Cytoplasmic in microvascular endothelial cells. Upon angiogenesis,
CC       when endothelial cell tube formation is initiated, it is secreted (By
CC       similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AK009533; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AK017248; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY500995; AAR97616.1; -; mRNA.
DR   EMBL; AK008168; BAB25506.3; -; mRNA.
DR   EMBL; AK008399; BAB25648.3; -; mRNA.
DR   EMBL; AK009533; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK017248; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC027286; AAH27286.1; ALT_INIT; mRNA.
DR   EMBL; BC052410; AAH52410.1; -; mRNA.
DR   CCDS; CCDS26697.1; -.
DR   RefSeq; NP_079906.2; NM_025630.3.
DR   AlphaFoldDB; Q7TN31; -.
DR   SMR; Q7TN31; -.
DR   BioGRID; 211550; 2.
DR   STRING; 10090.ENSMUSP00000022189; -.
DR   iPTMnet; Q7TN31; -.
DR   PhosphoSitePlus; Q7TN31; -.
DR   EPD; Q7TN31; -.
DR   MaxQB; Q7TN31; -.
DR   PaxDb; 10090-ENSMUSP00000022189; -.
DR   ProteomicsDB; 296082; -.
DR   Ensembl; ENSMUST00000022189.9; ENSMUSP00000022189.9; ENSMUSG00000021681.9.
DR   GeneID; 66549; -.
DR   KEGG; mmu:66549; -.
DR   UCSC; uc007rmi.2; mouse.
DR   AGR; MGI:1913799; -.
DR   CTD; 55109; -.
DR   MGI; MGI:1913799; Aggf1.
DR   VEuPathDB; HostDB:ENSMUSG00000021681; -.
DR   eggNOG; KOG0154; Eukaryota.
DR   GeneTree; ENSGT00730000111121; -.
DR   HOGENOM; CLU_023817_1_0_1; -.
DR   InParanoid; Q7TN31; -.
DR   OMA; CGQEDHF; -.
DR   OrthoDB; 3086173at2759; -.
DR   PhylomeDB; Q7TN31; -.
DR   TreeFam; TF315789; -.
DR   BioGRID-ORCS; 66549; 2 hits in 75 CRISPR screens.
DR   ChiTaRS; Aggf1; mouse.
DR   PRO; PR:Q7TN31; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q7TN31; Protein.
DR   Bgee; ENSMUSG00000021681; Expressed in cleaving embryo and 260 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR   CDD; cd22686; FHA_AGGF1; 1.
DR   CDD; cd16164; OCRE_VG5Q; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   InterPro; IPR035624; AGGF1_OCRE.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR041591; OCRE.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR23106; ANGIOGENIC FACTOR WITH G PATCH AND FHA DOMAINS 1; 1.
DR   PANTHER; PTHR23106:SF24; ANGIOGENIC FACTOR WITH G PATCH AND FHA DOMAINS 1; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF17780; OCRE; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   Genevisible; Q7TN31; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; Angiogenesis; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; Phosphoprotein; Reference proteome; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   CHAIN           2..711
FT                   /note="Angiogenic factor with G patch and FHA domains 1"
FT                   /id="PRO_0000064496"
FT   DOMAIN          431..484
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   DOMAIN          616..662
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..85
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   MOD_RES         661
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N302"
FT   CONFLICT        247
FT                   /note="S -> C (in Ref. 2; AK009533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="V -> A (in Ref. 3; AAH27286)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="L -> M (in Ref. 3; AAH27286)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="A -> V (in Ref. 3; AAH27286)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="R -> Q (in Ref. 3; AAH27286)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   711 AA;  79445 MW;  1EEABAF35608F214 CRC64;
     MASEAPSPPS PSPPPPASPE PELAQLRRKV EKLERELRSC RRQVREVEKL LQHTERLYRN
     AESDNQELRT QVEELSKILH CGKNEDNPKS DVEVQTESQA PWAISDYYYQ TCYNDDSLPS
     KETELCVQQS QCAQASALDP QDESHIDSGS YAGADATEGV SHRQEDAVTS DSQESVSALA
     EGPALEGSSL AESLRAAAEA AVSQTGFTYD ESTGLYFDHS TGFYYDSENQ LYYDPSTGIY
     YYCDVESGRY QFHSRVDLQP YQTSSTKPNR ERRLKKRRKE PGFYTANEEK DLSSEDQKVC
     SVEYINCSED EHSGNVKKKA RTDTSHKSSP LQLTVAVSGD TVESPGDDNS ASSKDERIGE
     SESEPEEGEI TDSQSEKSYD GDSSSGDRET SEESDDEDEE RIWPPCIRVI VIRSPVLQMG
     SLFIITAVSP ATIGREKDME HTVRIPEVAV SKFHAEVYFD HDLQSYVLVD QGSQNGTIVN
     GKQILQPKTK CDPYVLEHGD EVKIGETVLS FHIHPGSETC DGCEPGQVRA HLRLDRKDEP
     LVGPALSKEE KELERRKALK KIRVKYGLQN TDYEAEKALK NPKYKDRAGK RREQVGSEGT
     FQRDDAPASV HSEITDSNKG RKMLEKMGWK RGEGLGKDGG GMKTPIQLQL RRTHAGLGTG
     KLSSIDDVHL IQNKSKKHWD KARERFAETF TENKPRKETP GAVPWVTGTA E
//