KATL1_RAT
ID KATL1_RAT Reviewed; 488 AA.
AC Q5XIK7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Katanin p60 ATPase-containing subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE Short=Katanin p60 subunit A-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03024};
DE AltName: Full=p60 katanin-like 1 {ECO:0000255|HAMAP-Rule:MF_03024};
GN Name=Katnal1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates microtubule dynamics in Sertoli cells, a process
CC that is essential for spermiogenesis and male fertility. Severs
CC microtubules in an ATP-dependent manner, promoting rapid reorganization
CC of cellular microtubule arrays (By similarity). Has microtubule-
CC severing activity in vitro (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000250|UniProtKB:Q9BW62}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03024};
CC -!- SUBUNIT: Interacts with KATNB1 and KATNBL1.
CC {ECO:0000250|UniProtKB:Q9BW62}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03024}. Cytoplasm {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9BW62}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BW62}. Note=Colocalizes
CC with microtubules throughout the basal and adluminal compartments of
CC Sertoli cells (By similarity). Localizes within the cytoplasm,
CC partially overlapping with microtubules, in interphase and to the
CC mitotic spindle and spindle poles during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000250|UniProtKB:Q9BW62}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. A-like 1 sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03024}.
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DR EMBL; BC083673; AAH83673.1; -; mRNA.
DR RefSeq; NP_001006957.1; NM_001006956.1.
DR RefSeq; XP_003751164.1; XM_003751116.4.
DR RefSeq; XP_006248878.1; XM_006248816.3.
DR RefSeq; XP_006248879.1; XM_006248817.3.
DR RefSeq; XP_006248886.1; XM_006248824.3.
DR RefSeq; XP_017453776.1; XM_017598287.1.
DR RefSeq; XP_017453970.1; XM_017598481.1.
DR RefSeq; XP_017453971.1; XM_017598482.1.
DR RefSeq; XP_017459908.1; XM_017604419.1.
DR RefSeq; XP_017459909.1; XM_017604420.1.
DR RefSeq; XP_017459910.1; XM_017604421.1.
DR RefSeq; XP_017459911.1; XM_017604422.1.
DR RefSeq; XP_017459912.1; XM_017604423.1.
DR AlphaFoldDB; Q5XIK7; -.
DR SMR; Q5XIK7; -.
DR STRING; 10116.ENSRNOP00000001219; -.
DR iPTMnet; Q5XIK7; -.
DR PhosphoSitePlus; Q5XIK7; -.
DR PaxDb; Q5XIK7; -.
DR PRIDE; Q5XIK7; -.
DR Ensembl; ENSRNOT00000077328; ENSRNOP00000068753; ENSRNOG00000047618.
DR GeneID; 288449; -.
DR KEGG; rno:288449; -.
DR UCSC; RGD:1359252; rat.
DR CTD; 84056; -.
DR RGD; 1359252; Katnal1.
DR eggNOG; KOG0738; Eukaryota.
DR GeneTree; ENSGT00940000156630; -.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q5XIK7; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q5XIK7; -.
DR TreeFam; TF323170; -.
DR PRO; PR:Q5XIK7; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000916; Expressed in cerebellum and 10 other tissues.
DR ExpressionAtlas; Q5XIK7; baseline.
DR Genevisible; Q5XIK7; RN.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008352; C:katanin complex; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; ISS:UniProtKB.
DR GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR HAMAP; MF_03024; Katanin_p60_AL1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR028594; Katnal1_chordates.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..488
FT /note="Katanin p60 ATPase-containing subunit A-like 1"
FT /id="PRO_0000084603"
FT REGION 128..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW62"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 488 AA; 55201 MW; 0ED5B66744EEBCD6 CRC64;
MNLAEICENA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSLRDPATKA KWQQVRQELL
EEYEQVKSIV STLESFKMDK PPDFPVSCRD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
RPLRKDMGAG ARGLVGRAHQ ISKSDKAASR DKDYRARGRD DKARKNMQDG ASDGEIPKFD
GAGYDKDLVE ALERDIVSRN PSIHWDDIAD LEEAKKLLRE AVVLPMWMPD FFKGIRRPWK
GVLMVGPPGT GKTMLAKAVA TECGTTFFNV SSSTLTSKYR GESEKLVRLL FEMARFYAPT
TIFIDEIDSI CSRRGTSDEH EASRRVKSEL LIQMDGVGGA LENDDPSKMV MVLAATNFPW
DIDEALRRRL EKRIYIPLPT AKGRAELLKI SLREVELDPD IHLEDIAEKT EGYSGADITN
ICRDASLMAM RRRINGLSPE EIRALSKEEL QMPVTRGDLE LALKKIAKSV SAADLEKYEK
WMVEFGSA
