ID   A0A158P2D3_ATTCE        Unreviewed;      1005 AA.
AC   A0A158P2D3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Hyaluronan-mediated motility receptor C-terminal domain-containing protein {ECO:0000259|Pfam:PF15908};
GN   Name=105627264 {ECO:0000313|EnsemblMetazoa:XP_012063941.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012063941.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012063941.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; ADTU01007116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012063941.1; XM_012208551.1.
DR   AlphaFoldDB; A0A158P2D3; -.
DR   SMR; A0A158P2D3; -.
DR   STRING; 12957.A0A158P2D3; -.
DR   EnsemblMetazoa; XM_012208551.1; XP_012063941.1; LOC105627264.
DR   GeneID; 105627264; -.
DR   KEGG; acep:105627264; -.
DR   eggNOG; KOG0833; Eukaryota.
DR   InParanoid; A0A158P2D3; -.
DR   OrthoDB; 2788098at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR026203; IHABP.
DR   PANTHER; PTHR18956; HYALURONAN MEDIATED MOTILITY RECEPTOR; 1.
DR   PANTHER; PTHR18956:SF6; HYALURONAN MEDIATED MOTILITY RECEPTOR; 1.
DR   Pfam; PF15908; HMMR_C; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          852..970
FT                   /note="Hyaluronan-mediated motility receptor C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15908"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          119..160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          219..360
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          393..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          599..672
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          734..919
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        80..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  117505 MW;  69B8FF21D649F4F0 CRC64;
     MSFSKARIQR FNEFGSDAPP PGFYDPKFDN KVKGAIIEKS DRFLDNKSIS SAECNASVAS
     IKSSATAPIF RVPQPPPKRL ITKSTGSNYP KLKTPQPLTK NQNMKYESNQ QLADLQVECL
     NKDKTIQEHE KHIEDMKDEI RKLETELEEL RKKQDEIETQ HMKDIETMAK LQQDVINSHD
     DKHQVEMQTF RSQLLEMTKE KEREISSRKA MEKELRSRAT ELSKGITTLE AELNAKKEEN
     RIKIEALETH IEELLNKLEI VKRDRDIEIE LLQKEKCQLD VYVTNLTQER SNLESTLEIK
     QNEISKLEAE LSALQRKSQE LKEQYGELAD SYVHKISDFT NKHEEEIKHL KNDFLKEKEE
     LLMQNEVYKE CASNMETKAN NIEEINCSLA EELKNLQNIH TDVSQRLQEA QNELKLSNER
     HNTMMEKYKK DFIDMTNTHA ENKLKLEKVL EDAADEYFRE IENIKKIKDE EIEELKRTSG
     KKIEEETEQI IKHAQKMIEQ MEADKRDTLI ACRTESTEQV KKTIIECDAK VNAMVEEARN
     TVEEEMRFAN DNYKRCLLRM EVERAALDEK LSQRDIEITK LSTTLEELRS SVETQASFSQ
     SLQTELDKAE SELAEKKQEL RALKDHIRTE AAEMVARKKR FELIMAENQA SVAALTNRLA
     QSNAEVERLQ YEIKRGEDCI REHKELLTAM RSNSQLVHEQ VNSFMKDLDA HRDLVDQHQS
     GNISQFDSLK SIFETKIQNL KQNAAKEITR LEDDSKLKTI LNNELRIQLE EMTKSISEAQ
     SALLVLEEQN DAREIDISRM QLENNKILDQ LESSEKALEE NKRLLQNQAK QHKIITNEAN
     SRIEELSEKA KQFEEIEKTA KETTLLLEQE RIKWKSSENE LIQQLKEEIT RREEAEEEIK
     KLVTMNEVLK KEYKEVIEKY ADVIGHQNPK QRIKHVIRLK DKNYELEQEL LTKTRLVEQQ
     QKTIEKLKAE EKRSHWKGKE NVGMVHSTPI SSPHKTLTPL RDRND
//