AGGF1_MOUSE
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 03-AUG-2022, entry version 133.
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; Q7TN31; -.
DR PRIDE; Q7TN31; -.
DR ProteomicsDB; 296082; -.
DR Ensembl; ENSMUST00000022189; ENSMUSP00000022189; ENSMUSG00000021681.
DR GeneID; 66549; -.
DR KEGG; mmu:66549; -.
DR UCSC; uc007rmi.2; mouse.
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; FAENFQD; -.
DR OrthoDB; 683607at2759; -.
DR PhylomeDB; Q7TN31; -.
DR TreeFam; TF315789; -.
DR BioGRID-ORCS; 66549; 2 hits in 70 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 257 other tissues.
DR Genevisible; Q7TN31; MM.
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; cd00060; FHA; 1.
DR CDD; cd16164; OCRE_VG5Q; 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 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; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50174; G_PATCH; 1.
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
