AF1L1_HUMAN
ID AF1L1_HUMAN Reviewed; 768 AA.
AC Q8TED9; Q08AN4; Q08AN5; Q8IW82; Q8N8Z5; Q8N9Q4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Actin filament-associated protein 1-like 1;
DE Short=AFAP1-like protein 1;
GN Name=AFAP1L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Skin;
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).
RN [4]
RP FUNCTION, INTERACTION WITH CTTN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21333378; DOI=10.1016/j.ejcb.2010.11.016;
RA Snyder B.N., Cho Y., Qian Y., Coad J.E., Flynn D.C., Cunnick J.M.;
RT "AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with
RT cortactin and localizes to invadosomes.";
RL Eur. J. Cell Biol. 90:376-389(2011).
CC -!- FUNCTION: May be involved in podosome and invadosome formation.
CC {ECO:0000269|PubMed:21333378}.
CC -!- SUBUNIT: Interacts with CTTN. {ECO:0000269|PubMed:21333378}.
CC -!- INTERACTION:
CC Q8TED9; O95257: GADD45G; NbExp=8; IntAct=EBI-1053644, EBI-448202;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21333378}. Cell
CC projection, podosome {ECO:0000269|PubMed:21333378}. Cell projection,
CC invadopodium {ECO:0000269|PubMed:21333378}. Cytoplasm, cytoskeleton,
CC stress fiber {ECO:0000269|PubMed:21333378}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TED9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TED9-2; Sequence=VSP_026859;
CC Name=3;
CC IsoId=Q8TED9-3; Sequence=VSP_026857, VSP_026858;
CC Name=4;
CC IsoId=Q8TED9-4; Sequence=VSP_026856;
CC -!- TISSUE SPECIFICITY: Expressed in breast, colon and brain. In all 3
CC tissues, expressed in the microvasculature (at protein level). In
CC addition, in the breast, found in the contractile myoepithelial cell
CC layer which surrounds the breast ducts (at protein level). In the
CC colon, expressed in the mucous membrane and colonic crypts and in the
CC smooth muscle cell layer which provide movement of the colon (at
CC protein level). In the cerebellum, localized around the Purkinje
CC neurons and the granule cells of the granular layer, but not inside
CC cell bodies (at protein level). Outside of the cerebellar cortex,
CC expressed in glial cells (at protein level). Highly expressed away from
CC the cell bodies within the dentate nucleus (at protein level).
CC {ECO:0000269|PubMed:21333378}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK074185; BAB85011.1; ALT_INIT; mRNA.
DR EMBL; AK094067; BAC04277.1; -; mRNA.
DR EMBL; AK095980; BAC04664.1; -; mRNA.
DR EMBL; BC040723; AAH40723.1; -; mRNA.
DR EMBL; BC125093; AAI25094.1; -; mRNA.
DR EMBL; BC125094; AAI25095.1; -; mRNA.
DR CCDS; CCDS34274.1; -. [Q8TED9-1]
DR CCDS; CCDS54932.1; -. [Q8TED9-2]
DR RefSeq; NP_001139809.1; NM_001146337.2. [Q8TED9-2]
DR RefSeq; NP_001309991.1; NM_001323062.1.
DR RefSeq; NP_001309992.1; NM_001323063.1. [Q8TED9-3]
DR RefSeq; NP_689619.1; NM_152406.3. [Q8TED9-1]
DR AlphaFoldDB; Q8TED9; -.
DR SMR; Q8TED9; -.
DR BioGRID; 126390; 16.
DR IntAct; Q8TED9; 4.
DR STRING; 9606.ENSP00000296721; -.
DR iPTMnet; Q8TED9; -.
DR PhosphoSitePlus; Q8TED9; -.
DR BioMuta; AFAP1L1; -.
DR DMDM; 156630522; -.
DR EPD; Q8TED9; -.
DR jPOST; Q8TED9; -.
DR MassIVE; Q8TED9; -.
DR MaxQB; Q8TED9; -.
DR PaxDb; Q8TED9; -.
DR PeptideAtlas; Q8TED9; -.
DR PRIDE; Q8TED9; -.
DR ProteomicsDB; 74452; -. [Q8TED9-1]
DR ProteomicsDB; 74453; -. [Q8TED9-2]
DR ProteomicsDB; 74454; -. [Q8TED9-3]
DR ProteomicsDB; 74455; -. [Q8TED9-4]
DR Antibodypedia; 2023; 73 antibodies from 20 providers.
DR DNASU; 134265; -.
DR Ensembl; ENST00000296721.9; ENSP00000296721.4; ENSG00000157510.14. [Q8TED9-1]
DR Ensembl; ENST00000515000.1; ENSP00000424427.1; ENSG00000157510.14. [Q8TED9-2]
DR GeneID; 134265; -.
DR KEGG; hsa:134265; -.
DR MANE-Select; ENST00000296721.9; ENSP00000296721.4; NM_152406.4; NP_689619.1.
DR UCSC; uc003lqh.4; human. [Q8TED9-1]
DR CTD; 134265; -.
DR DisGeNET; 134265; -.
DR GeneCards; AFAP1L1; -.
DR HGNC; HGNC:26714; AFAP1L1.
DR HPA; ENSG00000157510; Tissue enhanced (skeletal).
DR MIM; 614410; gene.
DR neXtProt; NX_Q8TED9; -.
DR OpenTargets; ENSG00000157510; -.
DR PharmGKB; PA162375772; -.
DR VEuPathDB; HostDB:ENSG00000157510; -.
DR eggNOG; ENOG502R3HG; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_1_0_1; -.
DR InParanoid; Q8TED9; -.
DR OMA; QCNNTEG; -.
DR OrthoDB; 256810at2759; -.
DR PhylomeDB; Q8TED9; -.
DR TreeFam; TF332622; -.
DR PathwayCommons; Q8TED9; -.
DR SignaLink; Q8TED9; -.
DR BioGRID-ORCS; 134265; 6 hits in 1063 CRISPR screens.
DR ChiTaRS; AFAP1L1; human.
DR GenomeRNAi; 134265; -.
DR Pharos; Q8TED9; Tbio.
DR PRO; PR:Q8TED9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TED9; protein.
DR Bgee; ENSG00000157510; Expressed in apex of heart and 132 other tissues.
DR Genevisible; Q8TED9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR030113; AFAP.
DR InterPro; IPR030112; AFAP1L1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14338; PTHR14338; 1.
DR PANTHER; PTHR14338:SF1; PTHR14338:SF1; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..768
FT /note="Actin filament-associated protein 1-like 1"
FT /id="PRO_0000295239"
FT DOMAIN 220..316
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 418..512
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 82..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 611..700
FT /evidence="ECO:0000255"
FT COMPBIAS 111..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT MOD_RES 557
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT VAR_SEQ 1..385
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026856"
FT VAR_SEQ 341..377
FT /note="RLSQEKQTSDSDSVGVGDNCSTLGRRETCDHGKGKKS -> VYLSPLSLPQA
FT RQWPLNTGSTPGELTGWGESQATAKL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026857"
FT VAR_SEQ 378..768
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026858"
FT VAR_SEQ 719..761
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026859"
FT CONFLICT 84
FT /note="R -> Q (in Ref. 2; BAC04664)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="R -> C (in Ref. 2; BAC04664)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="E -> G (in Ref. 2; BAC04664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 86432 MW; 5DC1B952E797110F CRC64;
MDRGQVLEQL LPELTGLLSL LDHEYLSDTT LEKKMAVASI LQSLQPLPAK EVSYLYVNTA
DLHSGPSFVE SLFEEFDCDL SDLRDMPEDD GEPSKGASPE LAKSPRLRNA ADLPPPLPNK
PPPEDYYEEA LPLGPGKSPE YISSHNGCSP SHSIVDGYYE DADSSYPATR VNGELKSSYN
DSDAMSSSYE SYDEEEEEGK SPQPRHQWPS EEASMHLVRE CRICAFLLRK KRFGQWAKQL
TVIREDQLLC YKSSKDRQPH LRLALDTCSI IYVPKDSRHK RHELRFTQGA TEVLVLALQS
REQAEEWLKV IREVSKPVGG AEGVEVPRSP VLLCKLDLDK RLSQEKQTSD SDSVGVGDNC
STLGRRETCD HGKGKKSSLA ELKGSMSRAA GRKITRIIGF SKKKTLADDL QTSSTEEEVP
CCGYLNVLVN QGWKERWCRL KCNTLYFHKD HMDLRTHVNA IALQGCEVAP GFGPRHPFAF
RILRNRQEVA ILEASCSEDM GRWLGLLLVE MGSRVTPEAL HYDYVDVETL TSIVSAGRNS
FLYARSCQNQ WPEPRVYDDV PYEKMQDEEP ERPTGAQVKR HASSCSEKSH RVDPQVKVKR
HASSANQYKY GKNRAEEDAR RYLVEKEKLE KEKETIRTEL IALRQEKREL KEAIRSSPGA
KLKALEEAVA TLEAQCRAKE ERRIDLELKL VAVKERLQQS LAGGPALGLS VSSKPKSGET
ANKPQNSVPE QPLPVNCVSE LRKRSPSIVA SNQGRVLQKA KEWEMKKT
