ID   GCC2_RAT                Reviewed;        1679 AA.
AC   D3ZZL9;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=GRIP and coiled-coil domain-containing protein 2;
DE   AltName: Full=185 kDa Golgi coiled-coil protein;
GN   Name=Gcc2; Synonyms=Gcc185;
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 GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH RAB9A.
RX   PubMed=16885419; DOI=10.1091/mbc.e06-02-0153;
RA   Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M.,
RA   Pfeffer S.R.;
RT   "A functional role for the GCC185 golgin in mannose 6-phosphate receptor
RT   recycling.";
RL   Mol. Biol. Cell 17:4353-4363(2006).
CC   -!- FUNCTION: Golgin which probably tethers transport vesicles to the
CC       trans-Golgi network (TGN) and regulates vesicular transport between the
CC       endosomes and the Golgi. As a RAB9A effector it is involved in
CC       recycling of the mannose 6-phosphate receptor from the late endosomes
CC       to the TGN. May also play a role in transport between the recycling
CC       endosomes and the Golgi. Required for maintenance of the Golgi
CC       structure, it is involved in the biogenesis of noncentrosomal, Golgi-
CC       associated microtubules through recruitment of CLASP1 and CLASP2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts (via GRIP domain) with RAB6A
CC       (preferentially in its GTP-bound form). May interact (RAB6A-dependent)
CC       with ARL1; might be involved in GCC2 Golgi localization. Interacts with
CC       CLASP1 and CLASP2; recruits both proteins to membranes of the TGN.
CC       Interacts with STX16 (By similarity). Interacts (probably via GRIP
CC       domain) with RAB9A (preferentially in its GTP-bound form).
CC       {ECO:0000250, ECO:0000269|PubMed:16885419}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, trans-
CC       Golgi network membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
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DR   EMBL; AC114045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474016; EDL93092.1; -; Genomic_DNA.
DR   RefSeq; NP_001101103.1; NM_001107633.1.
DR   AlphaFoldDB; D3ZZL9; -.
DR   SMR; D3ZZL9; -.
DR   STRING; 10116.ENSRNOP00000001092; -.
DR   iPTMnet; D3ZZL9; -.
DR   PhosphoSitePlus; D3ZZL9; -.
DR   SwissPalm; D3ZZL9; -.
DR   jPOST; D3ZZL9; -.
DR   PaxDb; D3ZZL9; -.
DR   PeptideAtlas; D3ZZL9; -.
DR   PRIDE; D3ZZL9; -.
DR   GeneID; 309798; -.
DR   KEGG; rno:309798; -.
DR   UCSC; RGD:1305732; rat.
DR   CTD; 9648; -.
DR   RGD; 1305732; Gcc2.
DR   eggNOG; KOG0864; Eukaryota.
DR   HOGENOM; CLU_002922_0_0_1; -.
DR   InParanoid; D3ZZL9; -.
DR   PhylomeDB; D3ZZL9; -.
DR   TreeFam; TF332907; -.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:D3ZZL9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Proteomes; UP000234681; Chromosome 20.
DR   Genevisible; D3ZZL9; RN.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
DR   GO; GO:0034499; P:late endosome to Golgi transport; ISS:UniProtKB.
DR   GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR   GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0006622; P:protein targeting to lysosome; ISS:UniProtKB.
DR   GO; GO:0071955; P:recycling endosome to Golgi transport; ISS:UniProtKB.
DR   GO; GO:0070861; P:regulation of protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD.
DR   InterPro; IPR032023; GCC2_Rab_bind.
DR   InterPro; IPR000237; GRIP_dom.
DR   Pfam; PF01465; GRIP; 1.
DR   Pfam; PF16704; Rab_bind; 1.
DR   SMART; SM00755; Grip; 1.
DR   PROSITE; PS50913; GRIP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1679
FT                   /note="GRIP and coiled-coil domain-containing protein 2"
FT                   /id="PRO_0000401197"
FT   DOMAIN          1604..1654
FT                   /note="GRIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1466..1522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1569..1679
FT                   /note="Mediates interaction with RAB9A"
FT                   /evidence="ECO:0000250"
FT   REGION          1569..1608
FT                   /note="Mediates interaction with RAB6A"
FT                   /evidence="ECO:0000250"
FT   COILED          35..1469
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1466..1481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1482..1510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWJ2"
FT   MOD_RES         1474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWJ2"
FT   MOD_RES         1478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWJ2"
SQ   SEQUENCE   1679 AA;  195083 MW;  D208E89250B0CF22 CRC64;
     MEDSAQDAVT AAPSGTPKSK LETLPREDLI KFAKKQMMLL QKAKARCTEL DKEVEELKSK
     PVDGGTDDMI KVLTERLDAL LLEKAETEQQ CLCLKKENIK MKQEVEDSVT KLEETQKEFE
     QSHRNYVREM ESVKNELIAV HSEHSKEKAA LQRDLEGAVH RQAELLEQLK SQSDSEDNVK
     KLQEEIQNIT AAFEEQTSCL QKQLEATSDE KQQEIIHLQK VIEDNAQHYQ KDINTFQEEI
     VQLRATHKEE VNELMSQMET LAKEHEAAVN KLKENRVTLC ETSETIPENY QCESESLNED
     TSDASQENQK CSVALQEDPF AEHTVYDKVR QLEDSLKELE SQHSILKDEV TYMNNLKLKL
     EMDAQHIKDE FFHEREDLEF KINELLLAKE EQSYVVEKLK YEREDLNRQL CCTVEQHNKE
     IQRLQEHHQK EISELSETFM SGSEKEKLAL MFEIQGLKEQ CENLQHEKQE VVLNYESLRE
     MMEILQTELG ESAGKISQEF ETMKQQQASD VHELQQKLRT AFNEKDALLE TINRLQGENE
     KLLSQELVSE LESTMKNLKA DNSMYLASLG QKDTLLQELE AKISSLAEEK DDFISKIKTS
     REEIDDLHQK WEREQKLSVE LREAAEQAAQ HNSELRQRVS ELTGKLDEIL REKSQNDQNI
     MVQMKTMTED QEALSSKIKS LYEENNRLHS EKVQLSRDLE ALQSQQDFAY KEHVAEFEKK
     LQLMVEERDD LNKLLENEQL QKSFVKTQLY EFLKQMRPSI LEDNEEEDVV TVLKAVGESL
     VTVKEEKHNL VFEYDARVLE LERRIKCLQE ESVVQCEELR ALVRDSEQEK ILLRKELDEV
     TSTKEALQCD ILEMKNTNEK TSLENQTLST RVEELSRSLH SKNEVHNEKD LVIEHENLRL
     SLEQRESELQ DVRAELMLLK DSLEKSPSVK NDQLSLVKEL EEKIESLEKE SKDKDEKISK
     IKLVAVRAKK ELDSNRKEAQ TLRDELESVQ SEKDRLSASM KEFIQGAESY KNLLLEYDKQ
     SEQLDVEKER ANNFEHHIED LTKQLRDSTC QYEKLTSDNE DLLARIETLQ ANARLLEAQI
     LEVQRAKGVV EKELEAEKLQ KEQKIKEHVS TTNELEELQL QFQKEKKQLQ KTMQELELVK
     KDAQQTTLMN MEIADYERLM KELNQKLTNK NSKIEDLEQE MKIQKQKQET LQEEMTSLQS
     SVQHYEEKNA QIKQLLVKTK KELADAKQAE TDHLLLQASL KGELEASQQQ VEVYKIQLAE
     MTSEKHKIHE HLKTSAEQHQ RTLSAYQQRV VALQEESRTA KAEQAAVTSE FENYKVRVHN
     VLKQQKNKSV SQAETEGAKQ EREHLEMLID QLKIKLQDSQ NSLQISVSEF QTLQSEHDTL
     LERHNRMLQE TVTKEAELRE KLCSAQSENT MLKSEHAQTM CQLTSQNEAL RNSFRDQVRH
     LQDEHRKTVE TLQHQLSKVE TQLFQLKSEP PTKSPASSHQ PSKSLRERRT TDLPLLDMHT
     VTREEGEGME TTDSESVSSA GTHIQSLEQL LSSPDSKLER LTEASLWHTE FTKEELAEKL
     SSTTKSADHL NGLLRETEAT NAILMEQIKL LKSEIRRLER NQEREKSVAN LEYLKNVLLR
     FIFLKPGSER ERLLPVIDTM LQLSPEEKGK LATVAQGEEE SASRSSGWAS YLHSWSGLR