1A1L1_HUMAN
ID 1A1L1_HUMAN Reviewed; 501 AA.
AC Q96QU6; B4E219; Q8WUL4; Q96LX5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
DE Short=ACC synthase-like protein 1;
GN Name=ACCS; Synonyms=PHACS;
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] {ECO:0000305, ECO:0000312|EMBL:AAK11482.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11470512; DOI=10.1016/s0378-1119(01)00533-9;
RA Koch K.A., Capitani G., Gruetter M.G., Kirsch J.F.;
RT "The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-
RT carboxylate synthase encodes a protein lacking that activity.";
RL Gene 272:75-84(2001).
RN [2] {ECO:0000312|EMBL:BAB71541.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea {ECO:0000312|EMBL:BAB71541.1};
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4] {ECO:0000312|EMBL:EAW68072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH20197.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-421.
RC TISSUE=Uterus {ECO:0000312|EMBL:AAH20197.1};
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 [6] {ECO:0000305}
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-221 AND LEU-393.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane-1-
CC carboxylate but is capable of catalyzing the deamination of L-
CC vinylglycine. {ECO:0000269|PubMed:11470512}.
CC -!- INTERACTION:
CC Q96QU6; Q96QU6: ACCS; NbExp=8; IntAct=EBI-743387, EBI-743387;
CC Q96QU6; P14927: UQCRB; NbExp=3; IntAct=EBI-743387, EBI-743128;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96QU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96QU6-2; Sequence=VSP_055800, VSP_055801;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
CC -!- CAUTION: Similar to plant 1-aminocyclopropane-1-carboxylate synthases
CC but lacks a number of residues which are necessary for activity.
CC {ECO:0000269|PubMed:11470512}.
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DR EMBL; AY026508; AAK11482.1; -; mRNA.
DR EMBL; AK057649; BAB71541.1; -; mRNA.
DR EMBL; AK304074; BAG64981.1; -; mRNA.
DR EMBL; AC134775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68072.1; -; Genomic_DNA.
DR EMBL; BC020197; AAH20197.1; -; mRNA.
DR CCDS; CCDS7907.1; -. [Q96QU6-1]
DR RefSeq; NP_001120691.1; NM_001127219.1. [Q96QU6-1]
DR RefSeq; NP_115981.1; NM_032592.3. [Q96QU6-1]
DR AlphaFoldDB; Q96QU6; -.
DR SMR; Q96QU6; -.
DR BioGRID; 124199; 10.
DR IntAct; Q96QU6; 3.
DR STRING; 9606.ENSP00000263776; -.
DR DrugBank; DB03214; Vinylglycine.
DR iPTMnet; Q96QU6; -.
DR PhosphoSitePlus; Q96QU6; -.
DR BioMuta; ACCS; -.
DR DMDM; 74717198; -.
DR jPOST; Q96QU6; -.
DR MassIVE; Q96QU6; -.
DR MaxQB; Q96QU6; -.
DR PaxDb; Q96QU6; -.
DR PeptideAtlas; Q96QU6; -.
DR PRIDE; Q96QU6; -.
DR ProteomicsDB; 5797; -.
DR ProteomicsDB; 77907; -.
DR Antibodypedia; 13193; 206 antibodies from 26 providers.
DR DNASU; 84680; -.
DR Ensembl; ENST00000263776.9; ENSP00000263776.8; ENSG00000110455.14. [Q96QU6-1]
DR GeneID; 84680; -.
DR KEGG; hsa:84680; -.
DR MANE-Select; ENST00000263776.9; ENSP00000263776.8; NM_032592.4; NP_115981.1.
DR UCSC; uc001mxx.3; human. [Q96QU6-1]
DR CTD; 84680; -.
DR DisGeNET; 84680; -.
DR GeneCards; ACCS; -.
DR HGNC; HGNC:23989; ACCS.
DR HPA; ENSG00000110455; Low tissue specificity.
DR MIM; 608405; gene.
DR neXtProt; NX_Q96QU6; -.
DR OpenTargets; ENSG00000110455; -.
DR PharmGKB; PA162375284; -.
DR VEuPathDB; HostDB:ENSG00000110455; -.
DR eggNOG; KOG0256; Eukaryota.
DR GeneTree; ENSGT00940000161101; -.
DR HOGENOM; CLU_017584_1_3_1; -.
DR InParanoid; Q96QU6; -.
DR OMA; HGIEYAT; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q96QU6; -.
DR TreeFam; TF354218; -.
DR PathwayCommons; Q96QU6; -.
DR SignaLink; Q96QU6; -.
DR BioGRID-ORCS; 84680; 7 hits in 1082 CRISPR screens.
DR ChiTaRS; ACCS; human.
DR GenomeRNAi; 84680; -.
DR Pharos; Q96QU6; Tbio.
DR PRO; PR:Q96QU6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96QU6; protein.
DR Bgee; ENSG00000110455; Expressed in right uterine tube and 118 other tissues.
DR ExpressionAtlas; Q96QU6; baseline and differential.
DR Genevisible; Q96QU6; HS.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030170; F:pyridoxal phosphate binding; NAS:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..501
FT /note="1-aminocyclopropane-1-carboxylate synthase-like
FT protein 1"
FT /id="PRO_0000318071"
FT REGION 480..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 323
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 117..158
FT /note="LSQRDMQRVEPSLLQYADWRGHLFLREEVAKFLSFYCKSPVP -> PPGGSG
FT QVPVFLLQEPSTPQTRECGCPEWWCLALLCSGHGAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055800"
FT VAR_SEQ 159..501
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055801"
FT VARIANT 59
FT /note="D -> N (in dbSNP:rs33952257)"
FT /id="VAR_048227"
FT VARIANT 134
FT /note="D -> E (in dbSNP:rs2018795)"
FT /id="VAR_048228"
FT VARIANT 221
FT /note="G -> E (in a breast cancer sample; somatic mutation;
FT dbSNP:rs35514614)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038685"
FT VARIANT 393
FT /note="S -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_038686"
FT VARIANT 421
FT /note="P -> L (in dbSNP:rs3107275)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038687"
FT CONFLICT 94
FT /note="N -> S (in Ref. 2; BAB71541)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="F -> L (in Ref. 2; BAB71541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57324 MW; 62C99045F0BF8D5E CRC64;
MFTLPQKDFR APTTCLGPTC MQDLGSSHGE DLEGECSRKL DQKLPELRGV GDPAMISSDT
SYLSSRGRMI KWFWDSAEEG YRTYHMDEYD EDKNPSGIIN LGTSENKLCF DLLSWRLSQR
DMQRVEPSLL QYADWRGHLF LREEVAKFLS FYCKSPVPLR PENVVVLNGG ASLFSALATV
LCEAGEAFLI PTPYYGAITQ HVCLYGNIRL AYVYLDSEVT GLDTRPFQLT VEKLEMALRE
AHSEGVKVKG LILISPQNPL GDVYSPEELQ EYLVFAKRHR LHVIVDEVYM LSVFEKSVGY
RSVLSLERLP DPQRTHVMWA TSKDFGMSGL RFGTLYTENQ DVATAVASLC RYHGLSGLVQ
YQMAQLLRDR DWINQVYLPE NHARLKAAHT YVSEELRALG IPFLSRGAGF FIWVDLRKYL
PKGTFEEEML LWRRFLDNKV LLSFGKAFEC KEPGWFRFVF SDQVHRLCLG MQRVQQVLAG
KSQVAEDPRP SQSQEPSDQR R
