GCC2_MOUSE
ID GCC2_MOUSE Reviewed; 1679 AA.
AC Q8CHG3; Q8BR44; Q8R2Q5; Q9CT45;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=GRIP and coiled-coil domain-containing protein 2;
DE AltName: Full=185 kDa Golgi coiled-coil protein;
DE Short=GCC185;
GN Name=Gcc2; Synonyms=Kiaa0336;
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] OF 1-769.
RC TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-443.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-1679.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PROTEIN SEQUENCE OF 970-977, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: 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
CC (probably via GRIP domain) with RAB9A (preferentially in its GTP-bound
CC form). Interacts with CLASP1 and CLASP2; recruits both proteins to
CC membranes of the TGN. Interacts with STX16 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8CHG3; Q8BH43: Wasf2; NbExp=6; IntAct=EBI-643470, EBI-643162;
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC027339; AAH27339.1; ALT_INIT; mRNA.
DR EMBL; AK011206; BAB27466.3; -; mRNA.
DR EMBL; AK045701; BAC32463.2; -; mRNA.
DR EMBL; AB093232; BAC41416.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q8CHG3; -.
DR SMR; Q8CHG3; -.
DR IntAct; Q8CHG3; 2.
DR STRING; 10090.ENSMUSP00000054033; -.
DR iPTMnet; Q8CHG3; -.
DR PhosphoSitePlus; Q8CHG3; -.
DR EPD; Q8CHG3; -.
DR jPOST; Q8CHG3; -.
DR MaxQB; Q8CHG3; -.
DR PaxDb; Q8CHG3; -.
DR PRIDE; Q8CHG3; -.
DR ProteomicsDB; 267778; -.
DR MGI; MGI:1917547; Gcc2.
DR eggNOG; KOG0864; Eukaryota.
DR InParanoid; Q8CHG3; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR ChiTaRS; Gcc2; mouse.
DR PRO; PR:Q8CHG3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CHG3; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:MGI.
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; Direct protein sequencing;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1679
FT /note="GRIP and coiled-coil domain-containing protein 2"
FT /id="PRO_0000190075"
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 1467..1521
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 31..1613
FT /evidence="ECO:0000255"
FT COMPBIAS 1467..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"
FT CONFLICT 440
FT /note="I -> M (in Ref. 2; AAH27339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1679 AA; 194445 MW; 6E2F84263E5E0103 CRC64;
MEDSAPDAVA AAPSGTPKSK LETLPREDLI KFAKKQMMLL QKAKARCTEL DKEVEELKSK
PVDGGTDDII KVLTERLDAL LLEKAETEQQ CLCLKKENVK MKQEVEDSVT KLEETHKEFE
QSHRNYVKEI ESCKNELMAV HSEHSKETAI LQKELEEAVH KQVELREQLK SQSDSEDNVR
KLQEEIQNIT AAFEEQISCL EKKLEATSDE KQQEIIHLQK VIEDKAQHYQ KDINTFQAEI
LQLRATHKEE VTELMSQIET SAKEHEAEIN KLKENRVTQC EASENIPEKY QCESENLNEV
ASDASPESQN CSVALQEDPS AEQTVCDKVR QLEDSLKELE SQHSILKDEV TYMNNLKLKL
EMDAQHIKDE FFHEREDLEF KINELLLAKE EQGYVVEKLK YEREDLNRQL CCAVEQHNKE
IQRLQEHHQK EVSELSETFI SGSEKEKLAL MFEIQGLKEQ CENLQHEKQE VVLNYESLRE
MMEILQTELG ESAGKISQEF ETMKQQQASD VHELQQKLRS AFNEKDALLE TVNRLQGENE
KLLSQQELVP ELESTIKNLQ ADNSMYLASL GQKDTMLQEL EAKISSLAKE KDDFISKIKT
SHEEMDDLHQ KWEREQRLSV ELREAAGQAA QHNSELRQRV SELTGKLDEL VREKSQNDQS
ITVQMKTMTE DQEALSSKIK SLYEENNRLH SEKAQLSRDL EALQAQQDFA HKEHVAEFEK
KLQLMVEERD DLNKLLENEQ VQKSFVKTQL YEYLKQLRAS ILEENEEEDV VKLIQAVGES
LVKVKEEEHN LVFEYDARVL ELENKIKCLQ EDSAVQCEEL RTLVRDSEQE KILLRKELDA
VTSAKEALQL DLLEMKNTNE KASLENQTLS TQVEELSQTL HSRNEVHDEK VLVIEHENLR
LLLKQRESEL QDVRAELILL KDSLEKSPSV KDQLSLVKEL EEKIESLEKE SKDKDEKISK
IKLVAVKAKK ELDSNRKEAQ TLREELESVR SEKDRLSASM KEFLQGAESY KSLLLEYDKQ
SEQLDVEKER AHNFERHIED LTKQLRNSTC QYERLTSDNE DLLARIETLQ ANAKLLEAQI
LEVQKAKGVV EKELDAEELQ KEQKIKEHVS TVNELEELQL QFQKEKKQLQ KTMQELELVK
KDAQQTTLMN MEIADYERLM KELNQKLTNK NSTIEDLEQE MKIQKEKQET LQEEITSLQS
SVQHYEEKNT KIKQLLVKTK KELADAKQAE TDHLLLQASL KGELEASQQQ VEVYKIQLAE
MTSEKHKIHE HLKTSAEQHQ RTLSAYQQRV VALQEESRAA KAEQAAVTSE FESYKVRVHN
VLKQQKNKSV SQVETEGAKQ EREHLEMLID QLKIKLQDSQ NSLQISVSEY QTLQAEHDTL
LERHNRMLQE TVTKEAELRE KLCSVQSENT MMKSEHSQTM CQLTSQNEAL RTSFRDQVRH
LQDEHRKTVE TLQHQLSKLE AQLFQLKSEP STRSPASSHQ PSKSLRERRT TDLPLLDMHT
VAREEGEGME TTDSESVSSA GTHIQSLEQL LSSPDTKLER LAETSLWHNE FTKEELAEKL
SSTTKSADHL NGLLRETEAT NAILMEQIKL LKSEIRRLER NQEREKSVAN LEYLKNVLLR
FIFLKPGSER ERLLPVIDTM LQLSPEEKGK LATVAQGEEE SASRSSGWAS YLHSWSGLR
