WHAMM_MOUSE
ID WHAMM_MOUSE Reviewed; 793 AA.
AC Q571B6; Q80VK9; Q80YT0; Q8BJP8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=WASP homolog-associated protein with actin, membranes and microtubules;
DE AltName: Full=WAS protein homology region 2 domain-containing protein 1;
DE Short=WH2 domain-containing protein 1;
GN Name=Whamm; Synonyms=Kiaa1971, Whdc1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 96-793 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-471 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
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 [4]
RP FUNCTION.
RX PubMed=18614018; DOI=10.1016/j.cell.2008.05.032;
RA Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.;
RT "WHAMM is an Arp2/3 complex activator that binds microtubules and functions
RT in ER to Golgi transport.";
RL Cell 134:148-161(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a nucleation-promoting factor (NPF) that stimulates
CC Arp2/3-mediated actin polymerization both at the Golgi apparatus and
CC along tubular membranes. Involved as a regulator of Golgi positioning
CC and morphology. Its activity in membrane tubulation requires F-actin
CC and interaction with microtubules. Proposed to use coordinated actin-
CC nucleating and microtubule-binding activities of distinct WHAMM
CC molecules to drive membrane tubule elongation; when MT-bound can
CC recruit and remodel membrane vesicles but is prevented to activate the
CC Arp2/3 complex. Required for RhoD-dependent actin reorganization such
CC as in cell adhesion and cell migration (By similarity). Participates in
CC vesicle transport between the reticulum endoplasmic and the Golgi
CC complex. {ECO:0000250|UniProtKB:Q8TF30, ECO:0000269|PubMed:18614018}.
CC -!- SUBUNIT: Interacts with ACTR3; indicative for an association with the
CC ARP2/3 complex. Associates with microtubules; in vitro binds to tubulin
CC heterodimer in a 1:1 stoichiometry; decorates microtubules with a
CC repeat of 80 A along protofilaments. Interacts with RHOD (in GTP-bound
CC form). {ECO:0000250|UniProtKB:Q8TF30}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TF30}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:Q8TF30}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8TF30}. Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:Q8TF30}. Note=Localized to a perinuclear
CC compartment near the microtubule-organizing center (MTOC). Also
CC detected on tubulo-vesicular structures in the cell periphery that
CC frequently localized along microtubules.
CC {ECO:0000250|UniProtKB:Q8TF30}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q571B6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q571B6-2; Sequence=VSP_026722, VSP_026729;
CC -!- DOMAIN: The N-terminal region associates with membranes, the coiled-
CC coil region binds to microtubules and the WH2 domains promotes actin
CC nucleation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42749.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC38074.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAD90198.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220273; BAD90198.1; ALT_INIT; mRNA.
DR EMBL; BC042749; AAH42749.1; ALT_SEQ; mRNA.
DR EMBL; BC050804; AAH50804.1; -; mRNA.
DR EMBL; AK080911; BAC38074.1; ALT_SEQ; mRNA.
DR CCDS; CCDS52283.1; -. [Q571B6-1]
DR RefSeq; NP_001004185.3; NM_001004185.3. [Q571B6-1]
DR AlphaFoldDB; Q571B6; -.
DR SMR; Q571B6; -.
DR STRING; 10090.ENSMUSP00000128881; -.
DR iPTMnet; Q571B6; -.
DR PhosphoSitePlus; Q571B6; -.
DR EPD; Q571B6; -.
DR jPOST; Q571B6; -.
DR MaxQB; Q571B6; -.
DR PaxDb; Q571B6; -.
DR PeptideAtlas; Q571B6; -.
DR PRIDE; Q571B6; -.
DR ProteomicsDB; 299768; -. [Q571B6-1]
DR ProteomicsDB; 299769; -. [Q571B6-2]
DR Antibodypedia; 49806; 29 antibodies from 15 providers.
DR Ensembl; ENSMUST00000165460; ENSMUSP00000128881; ENSMUSG00000045795. [Q571B6-1]
DR Ensembl; ENSMUST00000209044; ENSMUSP00000146854; ENSMUSG00000045795. [Q571B6-2]
DR GeneID; 434204; -.
DR KEGG; mmu:434204; -.
DR UCSC; uc012fny.1; mouse. [Q571B6-1]
DR UCSC; uc012fnz.1; mouse. [Q571B6-2]
DR CTD; 123720; -.
DR MGI; MGI:2142282; Whamm.
DR VEuPathDB; HostDB:ENSMUSG00000045795; -.
DR eggNOG; ENOG502QPSI; Eukaryota.
DR GeneTree; ENSGT00510000046704; -.
DR HOGENOM; CLU_012316_1_0_1; -.
DR InParanoid; Q571B6; -.
DR OMA; CGQLERY; -.
DR OrthoDB; 183925at2759; -.
DR PhylomeDB; Q571B6; -.
DR TreeFam; TF331023; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 434204; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Whamm; mouse.
DR PRO; PR:Q571B6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q571B6; protein.
DR Bgee; ENSMUSG00000045795; Expressed in animal zygote and 206 other tissues.
DR ExpressionAtlas; Q571B6; baseline and differential.
DR Genevisible; Q571B6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0090527; P:actin filament reorganization; ISS:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0051127; P:positive regulation of actin nucleation; ISS:UniProtKB.
DR InterPro; IPR031738; JMY/WHAMM.
DR InterPro; IPR031808; JMY/WHAMM_N.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR026688; WHAMM.
DR PANTHER; PTHR23330:SF6; PTHR23330:SF6; 1.
DR Pfam; PF15871; JMY; 1.
DR Pfam; PF02205; WH2; 1.
DR Pfam; PF15920; WHAMM-JMY_N; 1.
DR PROSITE; PS51082; WH2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; Membrane; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..793
FT /note="WASP homolog-associated protein with actin,
FT membranes and microtubules"
FT /id="PRO_0000295101"
FT DOMAIN 698..716
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 728..745
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..253
FT /note="Mediates association with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q8TF30"
FT REGION 254..623
FT /note="Mediates interaction with microtubules"
FT /evidence="ECO:0000250|UniProtKB:Q8TF30"
FT REGION 556..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..793
FT /note="Mediates actin nucleation"
FT /evidence="ECO:0000250|UniProtKB:Q8TF30"
FT REGION 675..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..290
FT /evidence="ECO:0000255"
FT COILED 445..503
FT /evidence="ECO:0000255"
FT COILED 755..785
FT /evidence="ECO:0000255"
FT COMPBIAS 614..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..206
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026722"
FT VAR_SEQ 563..660
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026729"
FT CONFLICT 363
FT /note="E -> D (in Ref. 3; BAC38074)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> D (in Ref. 3; BAC38074)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="L -> S (in Ref. 3; BAC38074)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="T -> I (in Ref. 2; AAH42749)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="L -> P (in Ref. 2; AAH42749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 88997 MW; 326903DE5D6B84C8 CRC64;
MDSEQPDSLD GWVPLREDLF PEPERHQLRF LVAWNAAKGQ FAVTCHDRTA QRRRRERREA
GDGGCSWAGV LSPAGFRGAH RQLAALWPAL EPCFPPLPPE LDAASGAGWG LGRGLWALLW
PLLWPAPADP GDSALQELCR QLEHYLGLAA EGCGGATVRD VLFPAPGDSA DCEGLSEFRE
RTLRARLGQT ATRLHQVLQD HGKANTMVAL MKVYQEEDEL YQELVTMATT FFQYLLQPFR
DMREVATSCK LGILKSLDED ELGPRRVAAL QKEASEWTRQ AEEAVGSIQD ITVNYFKETV
TALTGMQKQM EQDQKRFGQA AWATAMPRLE NLKLMLARET LQLMRAKELC LKHRQAEIQR
KVEDLPRQGK QLDVVDELEI QCYEIQLELY DVKLEMLRNE ETILVTRLDS VKRLITEKQA
EVIYYDPCES PEELQSLAPD LELHLGDNRE LRALSQQCQR LEAQRGRICS RRALLRNRKD
HCRENHQLRL QQAKQSLRHL HQHHSIQMKR DKVKEEEQKK KEWIDHERQK TLERLRAYKE
KCPAHRSALK TTCSESMVSN LPGGRSQKRL STAHHHKTAH PASSKTGSAV PLPEASVRPP
EHQDPCGSVP VQAFVPVSDQ TLSGSSEDLS LPPQPPAPPL PPPPPPPPPP PLPPALSSFQ
GTTHQNLGLR TLATEDRPLP LACDPSAGRP CDYQGPGSMD EVLASLRQGK ASLRKVETPT
LPHPGTSVNE QVLAAIRQGV QLKKVHTGQG VDPGKKSTSD LERSIREALE RIKKVSADSE
EDNDEPSPTE WDR
